# hh: hedgehog location: 3-81. references: Nusslein-Volhard and Wieschaus, 1980, Nature 287: 795-801. Jurgens, Wieschaus, Nusslein-Volhard, and Kluding, 1984, Wilhelm Roux's Arch. Dev. Biol. 193: 283-95. Mohler and Wieschaus, 1985, Genetics 110: s35. Mohler, 1988, Genetics 120: 1061-72. Tearle and Nusslein-Volhard, 1987, DIS 66: 209-69. phenotype: A segment polarity type of embryonic lethal. Homozy- gous embryos have the posterior naked portion of the ventral surface of each segment deleted and replaced by a mirror image of the anterior denticle belts. Embryos appear to lack segmen- tal boundaries. In strong alleles, there is no obvious segmen- tation; the larvae are approximately 40% the length of the wild-type larvae, and there is a lawn of denticles arranged in a number of whorls on the ventral surface as a result of loss of naked cuticle. In intermediate alleles, naked cuticle is also lost from the ventral region, but the lawn of denticles is arranged in segmental arrays in mirror-image symmetry. The weak alleles show fusions that delete the naked cuticle usu- ally between abdominal segments 1 and 2 and 6, 7, and 8 (Mohler, 1988). Temperature shift experiments with a temperature-sensitive allele (viable and normal at 18, and mutant at 25) indicate two phases of hh activity at 25, the first during early embryogenesis (3-6 hr of development) and the second during the late larval and early pupal stages (4-7 days of development). alleles: allele origin synonym ref ( comments _______________________________________________________________ hh1 spont bar-3 1 viable hypomorph hh2 EMS hh6L 4 weak hh3 EMS hh6N 2-4 strong; ts hh4 EMS hh9K 2-4 weak; ts hh5 EMS hh10B 2-4 weak hh6 EMS hh11C 4 hh7 EMS hh11K 3 hh8 EMS hh13C 2-4 strong hh9 EMS hh13E 2-4 intermediate hh10 / ray hhGR1 3 In(3R)81F;94D10-E5; strong hh11 / ray hhGS1 3 In(3R)92B4-11;94D10-E5; strong hh12 / ray hhGS2 3 hh13 / ray hhGW1 3 hh14 / ray hhGW2 3 hh15 HD hhHL1 3 Tp(3R)85D;94D10-E5;97E7-8; strong hh16 HD hhHL2 3 hh17 HD hhHL3 3 hh18 EMS hhIIK 2-4 hh19 EMS hhIIO 2-4 hh20 EMS hhIIX 4 hh21 EMS hhIJ 2-4 strong hh22 TEM hhTW1 3 strong ( 1 = Ives, 1950, DIS 24: 58. 2 = Jurgens, Wieschaus, and Nusslein-Volhard, 1984, Wilhelm Roux's Arch. Dev. Biol. 193: 283-95; 3 = Mohler, 1988, Genetics 120: 1061-72; 4 = Tearle and Nusslein-Volhard, 1987, DIS 66: 209-69. cytology: Placed in 94E by segmental aneuploidy. Placed in 94D10-E5 based on breakpoint common to four hh rearrangements (Mohler, 1988). # hh1 phenotype: A weak hypomorphic allele that is not complemented by other hh alleles. Eye of homozygote small and narrow with about 150 facets. Eye disc size reduced; deep cleft at ante- rior edge cell; clusters at cleft look mature (Renfranz and Benzer, 1989, Dev. Biol. 136: 411-29). #*hi: high location: 2- (not located). origin: Found in Florida natural population. discoverer: Ives, 1943. references: 1943, Genetics 28: 77. 1950, Evolution 4: 236-52. phenotype: Male homozygous for hi produces sperm containing 10 times normal frequency of mutations. Heterozygous hi/+ causes a mutation rate 2-7 times normal. Ratio of sex-linked lethal to visible mutations about 8 to 1. Inversions associ- ated with about 5% of mutations. RK3. cytology: Salivary chromosomes normal. other information: Homozygous hi constructed by crossing two balanced lethal stocks, l1 hi/Cy X l2 hi/Cy. Since these stocks have developed a common lethal, it is now difficult to obtain hi homozygotes. #*Hi: Hirsute location: 3-{rearrangement}. origin: X ray induced. discoverer: Bishop, 1939. phenotype: All bristles except postscutellars and postdorsocen- trals multiplied, especially on head and anterior thorax. Eyes smaller and facets irregular. Homozygous lethal. RK2A. cytology: Associated with In(3LR)Hi = In(3LR)71A;91F. other information: Possibly the same as Brd. # Hia: Hiatus location: 2- (not located). origin: Spontaneous. discoverer: Bridges, 29b12. phenotype: Terminal interruption of L2. More obvious in heterozygous male than in heterozygous female. Homozygous viable. RK3. # Hid: see term # high: see hi # Himca: see Fs(2)Sz5 # Hin-d: see dpp # hindsight: see hnt # hir: heterochromatic-recombination-inducer location: 2- (left end of 2L). references: Hiraizumi, 1980, Genetics 94: s45-46. phenotype: Females homozygous for hir in combination with cer- tain cytoplasmic constitutions show increased recombination between lt and Rsp. Effect decreases with maternal age. hir without effect in males. # His: Histone location: 2-55 [between l(2)crc and lt]. references: Pardue, Kedes, Weinberg, and Bernstiel, 1977, Chro- mosoma 63: 135-51. Lifton, Goldberg, Karp, and Hogness, 1977, Cold Spring Harbor Symp. Quant. Biol. 42: 1047-51. phenotype: His refers collectively to five structural genes (His1, His2a, His2b, His3, and His4) for the five different histones (H1, H2A, H2B, H3, and H4). H2A, H2B, H3 and H4 par- ticipate in equimolar quantities in the formation of histone octomers, which form the protein core of nucleosomes. H1 associates with DNA between nucleosomes. The ratio of H1 to nucleosome core histones is higher in the salivary glands of larvae than in the cells of young embryos (Holmgren, Johans- son, Lambertsson, and Rasmusson, 1985, Chromosoma 93: 123- 31). For primary structure of H2B see Elgin, Schilling, and Hood (1979, Biochemistry 18: 5679-85). The expression of the histone genes changes in mid-embryogenesis (Ambrosio and Shedl, 1985, Dev. Biol. 111: 220-31; Ruddell and Jacobs- Lorena, 1986, Proc. Nat. Acad. Sci. USA 82: 3316-19). The egg chambers contain a variable and low level of mRNA during nurse cell polytenization; however, at the end of stage 10, all the nurse cells accumulate histone mRNA which is turned over to the growing oocytes as the nurse cells degenerate. Heterozygosity for full or partial deficiency of the histone genes suppresses variegation (BSV, Sbv, wm4); duplications without effect on level of variegation (Moore, Sinclair, and Grigliatti, 1983, Genetics 105: 327-44). Transcription not repressed by heat shock (Spradling, Pardue, and Penman, 1977, J. Mol. Bio. 109: 559-87). cytology: Localized to polytene bands 39D3 through 39E1-2 and possibly 39D2 as well by in situ hybridization of sea urchin histone messenger RNA (Pardue et al.). Orphon sequences homo- logous to His2B and His3 detected outside the tandem array but not localized further (Childs, Maxson, Cohn, and Kedes, 1981, Cell 23: 651-63). molecular biology: The five histone genes are deployed in the order His1 His3 His4 His2a His2b in a tandemly repeating unit that is represented in 100-200 copies per haploid complement. Units of 5.0 and 4.75 kb are found depending on whether or not there is a 250 base-pair insertion in the spacer region between His1 and His3 (Matsuo and Yamazaki, 1989, Nucleic Acids Research 17: 225-38); the 5 kb units are present from one to four times more frequently than 4.8 kb units, depending on the particular strain (Strausbaugh and Weinberg, 1982, Chromosoma 85: 489-505). Magnification and compensation of histone gene sequences in Df(2L)TW161 described by Chernyshev, Bashkirov, and Khesin (1980, Mol. Gen. Genet. 178: 663-68) and Chernyshev (1982, Mol. Biol. Moscow 16: 593-603). The repeating unit has been cloned, and the relative positions and directions of transcription of the five histone genes have been determined by Lifton et al. A 68 base-pair segment between His3 and His4 specifically binds the B transcription factor (Parker and Topol, 1984, Cell 36: 357-69). Sequence analysis by Goldberg (1979, PhD. Thesis, Stanford University) reveals the absence of introns. Among the first genes to be transcribed, transcription beginning 90 minutes after ovoposi- tion; transcription rates and message stability are high in early embryogenesis when the rate of DNA synthesis is maximal and both decrease markedly as development proceeds (Anderson and Lengyel, 1980, Cell 21: 717-27). When Drosophila tissue culture cells are heat shocked, H2B protein synthesis is increased, but H1, H2A, H3, and H4 protein synthesis is decreased (Farrell-Towt and Sanders, 1984, Mol. Cell Biol. 4: 2676-85). Histone messages non polyadenylated (Burkhardt and Birnstiel, 1978, J. Mol. Biol. 18: 61-79). Regular development of nucleosomes with respect to repeating sequence of histone genes studied by means of nuclease sensitivity (Samal, Worcel, Louis, and Schedl, 1981, Cell 23: 401-10). Bands, interbands, and puffs in the polytene chromosomes are recognized by a monoclonal antibody to an epitope in the carboxy-terminal tail of His1 (Hill, Watt, Wilson, Fifis, Underwood, Tribbick, Geysen, and Thomas, 1989, Chromosoma 98: 411-21). other information: One H2A-like sequence variant has been found (Donahue, Palmer, Condie, Sabatini, and Blumenfeld, 1986, Proc. Nat. Acad. Sci. USA 83: 4744-48). Within the H3 gene, the average nucleotide difference within a chromosome was 52% of that within a population (Matsuo and Yamazaki, 1989, Genetics 122: 87-97). # Hiv: see L(1)7C # Hirsute: see Hi hk: hook From Mohr, 1927, Hereditas 9: 169-79. # hk: hook location: 2-53.9. origin: Spontaneous. discoverer: Mohr, 24a4. references: 1927, Hereditas 9: 169-79 (fig.). phenotype: Bristles nearly all hooked at tip or blunted, some bent at right angles. Scutellars and verticals especially affected. Acrostichal hairs fewer and outer rows separated. Eyes slightly roughened. Wings usually divergent and may be smaller. Body sometimes small and chunky. Less extreme expression at 19, especially the wing character, but classifi- cation reliable. RK2. alleles: hk2 (Bridges, 33a31) spontaneous and less extreme than hk1. hk127 and hk131 X ray induced (Wright, Hodgetts, and Sherald, 1976, Genetics 84: 267-85). cytology: Located to 37B10-14 by deficiency analysis (Wright, Beermann, Marsh, Bishop, Seward, Black, Tomsett, and Wright, 1981, Chromosoma 83: 45-58). Df(2L)130/Df(2L)203 = Df(2L)37B9-C1;37D1-2/Df(2L)36E4-F1;37B9-C1 survives and is hk in phenotype (Wright et al.). # Hk: Hyperkinetic (J.C. Hall) location: 1-30.1. references: Kaplan and Trout, 1969, Genetics 61: 399-409. Ikeda and Kaplan, 1974, Amer. Zool. 14: 1055-66. Thompson, 1977, DIS 52: 2. Kaplan, 1979, Psychological Survey (Connolly, ed.). Allen and Unwin, London, Vol. 2, pp. 90-109. Stern and Ganetzky, 1989. J. Neurogenet. 5: 215-28. phenotype: Isolated as a dominant allele that induces ether- induced leg shaking in flies (Kaplan and Trout, 1969); later, hyperkinetic alleles showed recessive behavior, both in regard to the adult leg shaking phenotype and to the larval electro- physiological phenotype (Stern and Ganetzky, 1989). The vigorous leg shaking of flies can be induced by nitrogen or triethylamine, as well as ether, but not by chloroform (Ganetzky and Wu, 1982, Genetics 100: 597-614); ether also induces rhythmic bursts of impulses in certain cells of the thoracic ganglia of adults (summarized by Ikeda and Kaplan, 1974). The "patch clamp" experiments on neurons from Hk lar- vae reveals inward currents of unusually high conductance (Sun and Wu, 1985, Neurosci. Abstr. 11: 787). In Hk larvae, the amplitude and duration of the post synaptic response to a brief high frequency nerve stimulation is increased up to the level characteristic of Sh mutants (Stern and Ganetzky, 1989). Shadow stimuli induce jump response, which maps to the head in mosaic experiment (Kaplan, 1979). Hk can overcome heat- induced paralytic effects of parats (i.e. stobe light stimuli to the double mutant elicit jumps). Hk-induced leg shaking suppresseds by napts at its relatively low permissive tempera- ture (Ganetsky and Wu, 1982). Courtship performed by Hk males is abnormal (Burnet, Eastwood, and Connolly, 1974, Behav. Genet. 4: 227-35). Lifespan is shorter than normal and rate of oxygen consumption is greater than normal in Hk (Trout and Kaplan, 1970, Exper. Geront. 5: 83-93). Mutant focus of life-shortening effect maps to ventral anterior part of thorax as does leg shaking (Trout and Kaplan, 1982). Mutant shows weak orientation to spots in Y-maze test (Bulthoff, 1982, Biol. Cybernet 45: 63-7). alleles: allele origin discoverer synonym ref | ________________________________________________ Hk1 EMS Pasternak Hk1P 1, 2 Hk2 EMS Trout Hk2T 1 Hk3 spont Parris, 1973 Hk73 3 ( In addition to the alleles listed in the table, / ray- induced alleles have been isolated by Schlimgen on the basis of their failure to complement the leg shaking of Hk1 (Stern and Ganetzky, 1989). | 1 = Kaplan and Trout, 1969, Genetics 61: 399-409. 2 = Stern and Ganetzky, 1989, J. Neurogenet. 5: 215-28. 3 = Thompson, 1977, DIS 52: 2. cytology: Located in 9A-C since included in Df(1)Hk = Df(1)9A;9C (Stern and Ganetzky, 1989). # hl: see bxhl # hld: see hdp-a # Hm: see CbxHm under BSC # Hmg: Hmg-CoA-reductase location: 3-{81}. references: Gertler, Chiu, Richter-Mann, and Chin, 1988, Mol. Cell Biol. 8: 2713-21. phenotype: Encodes 3-methylglutaryl coenzyme A (HMG CoA) reduc- tase, the rate-controlling enzyme for cholesterol synthesis in mammals. In Drosophila melanogaster, the enzyme is not regu- lated by sterols (Brown, Havel, and Watson, 1983, J. Biol. Chem. 258: 8512-15; Silberkang, Havel, Friend, McCarthy, and Watson, 1983, J. Biol. Chem. 258: 8503-11); it synthesizes mevalonate for the production of nonsterol isoprenoids which are needed for growth and differentiation. The enzyme is found in cultured Kc and Schneider cells. cytology: Located in 95A. molecular biology: The gene was cloned and its nucleotide and putative amino acid sequences determined (Gertler et al., 1988). An open reading frame of 2,748 bp encodes a polypep- tide of 916 amino acids similar to hamster HMG CoA reductase; the C-terminal region showing 56% identical residues and the N-terminal region 32 to 60% identical residues. A 4 kb tran- script was found in early embryos, increased in abundance in late embryos, and was expressed at low levels in larvae, pupae, and adults; a 3.2 kb transcript was found at low levels in third-instar larvae, but increased in abundance in pupae and adults. Schneider cell fed mevalonate showed a reduction both in the 4 kb transcript and in enzyme activity. # hmr: hybrid male rescue location: 1-31.8 origin: Spontaneous in the Ukraine, USSR. references: Hutter and Ashburner, 1987, Nature 327: 331-33. phenotype: Rescues D. melanogaster / simulans hybrid males that would not survive in the absence of the gene. Hybrid males that carry both hmr and a duplication (thought to be hmr+) are lethal, so the rescue is considered recessive. The hybrids are sterile. Hybrid females from the reciprocal cross show low viability. D. melanogaster / mauritania and D. melanogas- ter / sechellia hybrid males also rescued. The rescue of D. melanogaster / simulans and D. melanogaster / mauritania males by hmr almost complete at 18; at 25 D. melanogaster / mauri- tania male rescue is good, but D. melanogaster / simulans males is poor at this temperature. At 18 only one third of the D. melanogaster / sechellia males are rescued. cytology: Located in bands 9D1-2;9E1-2. No chromosome abnor- malities are shown. # hn3: see Hnr2 # Hn: Henna location: 3-23.0 phenotype: A recessive eye color mutant, amorphic alleles of which show slight dominance. The first allele described, being associated with a deficiency, was homozygous lethal, and therefore only the slight dominant phenotype of homogenously dark, dull brown eye color could be scored; thus the dominant symbol Hn was applied. All subsequent alleles homozygous viable, exhibiting dark brown sepia-like or clot-like eyecolor in homozygous flies. Red pteridine eye pigments, drosopte- rins, reduced and sepiapterin accumulates; sepiapterin reduc- tase levels reduced (Barthelmess and Robertson, 1970, Genet. Res. 15: 65-86). Eye color of Hnr and Hnr3 autonomous in transplants of optic disk into wild-type hosts (Beadle and Ephrussi, 1936, Genetics 21: 230). Larval Malpighian tubes bright yellow as in wild type (Beadle, 1937, Genetics 22: 587-611). RK1 or 2 as homozygote. alleles: alleles origin discoverer ref ( ______________________________________________________ Hn1 | X ray Van Atta, 30k 1, 4, 8, 9 Hn53k ultraviolet Meyer, 53k 1, 5 Hnp / spont Craymer 2 Hnr spont Bridges, 33r20 1, 6 *Hnr2 ` Nordenskold, 33b9 1, 7 Hnr3 - spont Weinstein, 1927 1, 4 *Hnr53j ultraviolet Meyer, 53j 1, 5 *HnrI spont Ives, 45j17 1, 3 *HnrN spont Williamson, 53j 1, 10 ( 1 = CP627; 2 = Craymer, 1980, DIS 55: 197-200; 3 = Ives, 1946, DIS 20: 65; 4 = Lewis, 1956, DIS 30: 130; 5 = Meyer, 1954, DIS 28: 76; 6 = Mohr, 1937, DIS 8: 12; 7 = Norden- skold, 1937, DIS 7: 18; 8 = Van Atta, 1932, Am. Nat. 66: 93-95; 9 = Van Atta, 1932, Genetics 17: 637-59; 10 = Williamson, 1955, DIS 29: 75. | Associated with Df(3L)66A;66B; T(2;3)Hn=T(2;3)53E- 54A;77A;96A induced simultaneously but separable from Hn. / Present in most if not all TM6 chromosomes. ` Formerly bu: brunette. - Formerly sed: sepiaoid; Hnr3 more extreme than Hnr2. Homozygotes of Hnr3 and ry6 found to be viable (Thompson, 1983, DIS 54: 128-29). Hnr3 lacks tetrahydropterin and has increased levels of tetrohydrobiopterin (Guillamon and Ferre, 1988, Biochem. Biophys. Res. Commun. 152: 49-55). cytology: Placed in 66A-B on basis of its association with *Df(3L)Hn = Df(3L)66A;66B (Lewis, 1956, DIS 30: 130). # hn RNA-binding protein: see Hrb # hnt: hindsight location: 1-7. origin: Induced by ethyl methanesulfonate. references: Wieschaus, Nusslein-Volhard, and Jurgens 1984, Wilhelm Roux's Arch. Dev. Biol. 193: 296-307. phenotype: Homozygous embryonic lethal; no germ band retrac- tion; embryo U-shaped with head facing posteriorly. Germ line clones obtained; no maternal effect (Perrimon, Engstrom, and Mahowald, 1989, Genetics 121: 333-52). alleles: Three. cytology: Placed in 4B1-C15. # ho: see dppd-ho # Ho: see tbs # Hodos: see Fs(3)Sz10 # hold-up: see hwp # Homeobox 2.0: see H2.0 # homothorax: see hth # Hont: see Fs(2)Sz6 # hook: see hk # Hooked-veins: see Hv # hop: hopscotch location: 1-34.6 (between dsh and dlg). references: Perrimon and Mahowald, 1986a, Dev. Biol. 118: 28- 41. 1986b, Symp. Soc. Dev. Biol. 44: 221-35. phenotype: The wild-type allele of hop is required for the con- tinued cell division of all diploid cells as well as the establishment of the normal array of segments. Most of the mutants are homozygous late zygotic (L-P) lethals; one mutant is a larval lethal; two other mutants have some adult sur- vivors (hemizygous males being morphologaically normal, but 40% of the homzygous females and 85% of the hemizygous females showing major defects). Most of the heteroallelic females are lethal, with the following exceptions: genotype percent viable ____________________________ hop29/hop25 12% hop3/hop25 16% hop14/hop25 40% hop12/hop25 68% hop27/hop25 100% hop32/hop25 100% hop33/hop25 100% All viable heteroallelic combinations are female sterile, failing to produce eggs or laying abnormal eggs that are small, with a clear chorion and with chorionic filaments absent or partially fused (Perrimon and Mahowald, 1986a). There is a maternal effect on thoracic and abdominal segments, the most extreme embryos [produced from homozygous l(1)hop germline clones that have not received a paternal copy of hop+] showing defects in the posterior spiracles and in seg- ments T2 (denticle belt deleted). T3, A4, and A5 (segment missing) and A8 (segment reduced in size); the least extreme mutant embryos from germline clones show defects in segment A5. Defects visible in early segmentation stages. The extent of the defects is dependent on the strength of the maternal alleles and the paternal contribution. Wild-type sperm can rescue all defects, except those in A5. A few of the rescued progeny hatch and develop into adults. alleles: allele origin discoverer synonym ref ( comments ______________________________________________________________ hop1 X ray Lefevre l(1)L4 1, 4, 6 L-P lethal hop2 X ray Lefevre l(1)C111 5, 6 L-P lethal hop3 X ray Lefevre l(1)GA32 5, 6 L-P lethal hop4 X ray Lefevre l(1)HC257 5, 6 L-P lethal hop5 X ray Lefevre l(1)HC289 5 hop6 X ray Lefevre l(1)KC28 5 hop7 X ray Lefevre l(1)RA56 5 hop8 EMS Lefevre l(1)DA506 3 hop9 EMS Lefevre l(1)DC764 3 hop10 EMS Lefevre l(1)EA39 hop11 EMS Lefevre l(1)EF447 3 hop12 EMS Lefevre l(1)VA85 3, 6 L/MER hop13 EMS Lefevre l(1)VA108 3, 6 L-P lethal hop14 EMS Lefevre l(1)VA275 3, 6 L-P lethal hop15 EMS Lefevre l(1)VA312 3, 6 L-P lethal hop16 EMS Lefevre l(1)VE666 3, 6 L-P lethal hop17 EMS Lefevre l(1)VA928 3 hop18 EMS Geer l(1)v12 2 hop19 EMS Geer l(1)v20 2 hop20 EMS Geer l(1)v48 2 larval lethal hop21 EMS Geer l(1)v82 2 hop22 EMS Geer l(1)v109 2 hop23 EMS Geer l(1)v148 2 hop24 EMS Geer l(1)v223 2 hop25 EMS Geer ms(1)v1; msv1 1, 2, 6 viability and fertility poor in males and females | hop26 EMS Geer msn1 2 viability poor; male sterile hop27 ENU Voelker l(1)M4 6 L-P lethal hop28 ENU Voelker l(1)M10 hop29 ENU Voelker l(1)M13 6 L-P lethal hop30 ENU Voelker l(1)M25 hop31 ENU Voelker l(1)M28 hop32 ENU Voelker l(1)M38 6 L-P lethal hop33 ENU Voelker l(1)M75 6 L-P lethal hop34 EMS Perrimon l(1)9P5 6 L-P lethal hop35 EMS Perrimon l(1)1PP7 6 L-P lethal ( 1 = Dybas, Harden, Machnicki, and Geer, 1983, J. Exp. Zool. 226: 293-302; 2 = Geer, Lischwe, and Murphy, 1983, J. Exp. Zool. 225: 107-18; 3 = Lefevre. 4 = Lefevre, l971, Genetics 67: 497-513; 5 = Lefevre and Watkins, 1986, Genetics 113: 869-95; 6 = Perrimon and Mahowald, 1986, Dev. Biol. 118: 28-41. | Testes of hemizygous males are usually rudimentary and lack sperm; ovaries of homozygous and hemizygous females usually abnormal, lack egg chambers [believed to be somataic defect since eggs appear normal when allele is analyzed in germline clones (Perrimon and Mahowald, 1986a)]. cytology: Placed in 10B6-8 (Perrimon and Mahowald, 1986a); included in Df(1)N71 = Df(1)10B5;10D4 but not in Df(1)DA622 = Df(1)10B8;10D2. # Horka: see Fs(3)Sz11 # hp: humped location: 3- (rearrangement). origin: Spontaneous. discoverer: Bridges, 31a22. phenotype: Thorax shortened and strongly humped with thoracos- cutellar groove almost absent. Eyes sharply reduced, may be absent at 29. Bristles Minute-like and occasionally missing. Viability 10% wild type. RK3A. cytology: Associated with In(3R)P (Craymer). #*hpa: hyperantenna location: 1-50.1. origin: Induced by DL-p-N,N-di-(2-chloroethyl)amino- phenylalanine (CB. 3007). discoverer: Fahmy, 1954. references: 1959, DIS 33: 86. phenotype: Antennae enlarged or have duplicated parts, some- times an extra antennal base near the eye. Grossly deformed head and eyes. Wings have rounded tips and incised inner mar- gins. An occasional bristle absent or shorter. Phenotype variable; minimal expression shown by slightly altered eye shape and blunt wing tips. Males viable and infertile; females sterile. RK3. # Hpb: Hydroxyphenyl-buten-1 location: 2- (chromosomal location tentative). origin: Induced by ethyl methanesulfonate. references: Kikuchi, 1973, Nature 243: 36-38. phenotype: Flies carrying Hpb-1 are attracted to compounds that repel wild type. The strongest of these is 4- (0- Hydroxylphenyl)3-buten2-one, where 71% of mutant bearing flies respond positively and 67% of wild type flies negatively to the stimulus, an odds ratio of approximately 5. Slightly lower differentials are seen with eleven among 63 other com- pounds tested. # Hr: see dsxD # Hrb1: hnRNA-binding protein 1 (S. Haynes) location: 3-{98}. origin: Isolated from a cDNA library using pen repeat probe. references: Haynes, Raychaudhuri and Beyer, 1990, Mol. Cell. Biol. 10: 316-23. Haynes, Rebbert, Mozer, Forquignon, and Dawid, 1987, Proc. Natl. Acad. Sci. USA 84: 1819-23. phenotype: Homology to the mammalian A and B hnRNP proteins based on amino acid sequence inferred from nucleotide sequence. cytology: Placed in 98D-E by in situ hybridization. Located 15 kb distal of fkh. molecular biology: Genomic clone isolated from Maniatis library (partial sequence); cDNA clones from ovarian, embryonic and pupal libraries (complete sequences). Eight transcripts are produced by use of the alternative promoters, exons, and splice acceptor sites; these transcripts can encode four pro- tein isoforms. Transcripts are expressed throughout develop- ment with highest levels in ovaries, early embryos, and pupae. # Hrb2: hnRNA-binding protein 2 (S. Haynes) origin: Isolated from a cDNA library by homology with Droso- phila Hrb1 gene. references: Haynes, Raychaudhuri, Johnson, Amero, and Beyer, 1990, Mol. Biol. Rep. 14: 93-4. phenotype: Homology to the mammalian A and B hnRNP proteins based on amino acid sequence inferred from nucleotide sequence. cytology: Placed in 87F by in situ hybridization. molecular biology: Genomic clone isolated from Maniatis library (partial sequence); cDNA clones from ovarian, and embryonic libraries (complete sequences). Two transcripts (2.2 and 1.7 kb) are produced by use of alternative polyadenylation sites. Transcripts are expressed throughout development with highest levels in ovaries, early embryos, late larvae and early pupae. # Hsc70: Heat-shock-cognate 70 Three gene sequences that share homology with Hsp70 as demonstrated by in situ hybridization to polytene chromosomes and subsequent sequence determination. Although their tran- scription is developmentally regulated, it is temperature independent. Sequence analysis of the amino terminus reveals 70-80% identity between Hsp70 and its three cognates. Unlike Hsp70, the Hsc70 genes carry sequences in the 5 non-coding region that encode three additional amino acids. In Hsc70-1, the codon specifying amino acid 66 is interrupted by an 1.7 kb insertion; in Hsc70-2, the codon specifying amino acid 55 is also interrupted by an insertion (Craig et al., 1983). Hsc70-4 and Hsp70, however, have no insertions in the region coding for amino acids 1-101. transcript abundance locus cytology length ref ( embryo larva adult ________________________________________________________ Hsc70-1 70C 1.7 kb 1, 2 + - ++ Hsc70-2 | 87D 0.65 kb 1 - - + Hsc70-4 88E 1 ++++ ++++ ++++ ( 1 = Craig, Ingolia, and Manseau, 1983, Dev. Biol. 99: 418- 26; 2 = Ingolia and Craig, 1982, Proc. Nat. Acad. Sci. USA 79: 525-29. | Between ry and pic. # Hsp: Heat-shock protein Exposure of cells to pulses of elevated temperature ini- tiates the heat-shock response. A restricted subset of genes, the Hsp genes, is activated and the majority of transcription and translation is shut-down. However, mitochondrial- and histone-gene activities persist (Spradling, Pardue, and Pen- man, 1977, J. Mol. Biol. 109: 559-87). This response follows a pulse of 36 to 40; treatments above 40 inhibit all activity and lead to death; treatments of 30-35 induce heat-shock- protein synthesis without repressing normal protein synthesis (Tissieres, Mitchell, and Tracy, 1974, J. Mol. Biol. 84: 389-98). Similar response inducible by other stressful treatments. The response may be elicited at all stages of the life cycle and in cultured cells. Stage specific phenocopies result from heat shocking early stages of Drosophila develop- ment [Mitchell and Petersen, 1982, Heat Shock from Bacteria to Man (Schlesinger, Ashburner, and Tissieres, eds.). Cold Spring Harbor Laboratory, New York, pp. 345-52]. In polytene cells existing puffs regress and a novel group quickly appears [33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D (Ashburner, 1970, Chromosoma 31: 356-76; Tissieres et al., 1974)]. Activation of transcription of Hsp genes apparently involves the sequen- tial binding of two or more protein factors in vicinity of TATA box (Wu, 1984, Nature (London) 309: 229-34). Binding sites for these proteins are multiple short upstream sequence elements called HSEs or heat shock consensus elements (Pelham, 1982, Cell 30: 517-28; Xiao and Lis, 1988, Science 239: 1139-42). Polymerase II dissociates from most chromo- some regions and accumulates at the new puff sites (Bonner and Kerby, 1982, Chromosoma 85: 93-108). 3H-uridine incorporation ceases at its usual positions and commences at new puff sites. Preexisting polysomes disaggregate and within a few minutes a new population of polysomes appears containing newly transcribed mRNA; this RNA hybridizes to some of the heat- shock puffs. The effects of heat shock may be abrogated to some degree by pretreatment with a pulse of a slightly lower temperature (Mitchell, Moller, Petersen, and Lipps-Sarmiento, 1979, Dev. Genet. 1: 181-92 Peterson and Mitchell, 1981, Proc. Nat. Acad. Sci. USA 78: 1708-11). For reviews of the heat-shock response see Ashburner and Bonner (1978, Cell 17: 241-54) and Heat Shock from Bacteria to Man (cited above). The different heat-shock genes are designated by the molecular weights in kilodaltons of the polypeptides they produce: Hsp22, Hsp23, Hsp26, Hsp27, Hsp68, Hsp70 and Hsp83. gene location ref ( cytology _________________________________________________ Hsp22 | 3-{28} 1-3, 5, 10, 11 67B Hsp23 | 3-{28} 1-3, 5, 10, 11 67B Hsp26 | 3-{28} 1-3, 5, 10, 11 67B Hsp27 | 3-{28} 1-3, 5, 10, 11 67B Hsp-G1 / 3-{28} 1, 10 67B Hsp-G2 / 3-{28} 1, 10 67B Hsp-G3 / 3-{28} 1, 10 67B Hsp68 3-{81} 4 95D Hsp70 ` 3-{51} 4, 6-9 87A7;87C1 Hsp83 3-{5} 4 63B-C ( 1 = Ayme and Tissieres, 1985, EMBO J. 29: 49-54; 2 = Corces, Holmgren, Freund, Morimoto, and Meselson, 1980, Proc. Nat. Acad. Sci. USA 77: 5390-93; 3 = Craig and McCarthy, 1980, Nucleic Acids Res. 8: 4441-57; 4 = Holmgren, Livak, Morimoto, Freund, and Meselson, 1979, Cell 18: 1359-70; 5 = Ingolia and Craig, 1982, Proc. Nat. Acad. Sci. USA 79: 2360-64; 6 = Ish-Horowicz and Pinchon, 1980, J. Mol. Biol. 156: 21-35; 7 = Ish-Horowicz, Pinchon, Gausz, Gyurkovics, Bencze, Goldschmidt-Clermont, and Holden, 1979a, Cell 17: 565-717; 8 = Ish-Horowicz, Pinchon, Schedl, Artavanis-Tsakonas, and Mirault, 1979b, Cell 18: 1351-58; 9 = Mason, Torek, Kiss, Karch, and Udardy, 1982, J. Mol. Biol. 156: 21-35; 10 = Pauli, Arrigo, Vasquez, Tonka, and Tissieres, 1989, Genome 31: 671-76; 11 = Voellmy, Goldschmidt-Clermont, Southgate, Tessieres, Levis, and Gehr- ing, 1981, Cell 23: 261-70. | Located genetically 2.4 units to the right of h (Peterson, Moller, and Mitchell, 1979, Genetics 92: 891-902). / Synonym: gene1, gene2, gene3 [Southgate, Mirault, Ayme, and Tissieres, 1985, Changes in Gene Expression in Response to Environmental Stress (Atkinson and Walden, eds.). Academic Press, New York, pp. 1-30]; gene4 (=2), gene5 (=3) (Sirotkin and Davidson, 1982, Dev. Biol. 89: 196-210). ` Cytological location by deficiency mapping and in situ hybridization (Ish-Horowitz et al., 1979). # Hsp22 - Hsp-G3 phenotype: There are seven closely related heat-shock genes at 67B (Ayme and Tissieres, 1985; Pauli, Arrigo, Vasquez, Tonka, and Tissieres, 1989, Genome 31: 671-76). In addition to the four small heat-shock genes previously identified (Hsp22, Hsp23, Hsp26, and Hsp27), three more genes (Hsp-G1, Hsp-G2, and Hsp-G3, formerly called Gene1, Gene2, and Gene3) have been found clustered within 15 kb of DNA at the same 67B cytologi- cal location. All seven genes are heat-shock inducible in almost all cells at the stages tested (Ayme and Tissieres, 1985). The genes are also transcribed during certain develop- mental stages in the absence of heat shock (Sirotkin and Davidson, 1982, Dev. Biol. 89: 196-210). Pauli et al (1989) report that the maximum accumulation of developmental rRNA in a majority of these small heat-shock genes occurs in the white pupae stage; in Hsp-G2, however, a small transcipt is found in embryos, first and second instar larvae, and young pupae; and a larger transcript in the pupal and adult stages of males (Pauli and Tonka, 1987, J. Mol. Biol. 198: 235-40; Pauli, Tonka, and Ayme-Southgate, 1988, J. Mol. Biol. 200: 47-53). In absence of stress, the expression of Hsp26 has been observed in spermatocytes, nurse cells, epithelium, imaginal discs, proventriculus, and neurocytes (Glaser, Wolfner, and Lis, 1986, EMBO 5: 747-54). Transcripts of Hsp26 and Hsp27 accumulate in adult ovaries, apparently originating in nurse cells (Zimmerman, Petri, and Meselson, 1983, Cell 32: 1161- 70). alleles: A mutant alelle of Hsp27 that produces small amounts of a large, heat-induced transcript has been cloned and found to contain a defective P-element (Eissenberg and Elgin, 1987, Genetics 115: 333-40). molecular biology: All of the small heat-shock genes are located on the same 15 kb fragment. The order from distal to proximal is Hsp-G3, Hsp-G2, Hsp22, Hsp26, Hsp-G1, Hsp23, Hsp27, with Hsp22, Hsp-G1, and Hsp-G3 transcribed from one strand and the remainder transcribed from the other (Corces, Holmgren, Freund, Morimoto, and Meselson, 1980, Proc. Nat. Acad. Sci. USA 77: 5390-93; Voellmy, Goldschmidt-Clermont, Southgate, Tissieres, Levis, and Gehring, 1981, Cell 23: 261-70; Szauter and Pardue, 1982, Genetics 100: s67 68; Ayme and Tissieres, 1985; Pauli et al., 1989). Genomic and putative amino acid sequences obtained from all seven genes (Ingola and Craig, 1982, Proc. Nat. Acad. Sci. USA 79: 2360- 64; Southgate, Ayme, and Voellmy, 1983, J. Mol. Biol. 165: 35-57; Ayme and and Tissieres, 1985; Pauli and Tonka, 1987; Pauli et al., 1988). Activation of the small heat-shock genes by stress depends on consensus sequences upstream of the transcription start sites. A third and larger transcript is induced by heat shock in Hsp-G2; this transcript extends through Hsp22 to the 3 end of the latter gene (Pauli et al., 1988). Heat-shock proteins 22, 23, 26, and 27 are encoded by the corresponding genes; protein products of the other three heat-shock genes have not been identified yet, although the amino acid sequences have been estimated from genomic sequences. All seven genes show homologies, both to each other, and to a lesser extent, to mammalian lens protein, the (-crystallins. There is considerable upstream sequence iden- tity between heat-shock genes expressed strongly in ovaries [i.e., Hsp26, Hsp27, and the larger heat-shock gene Hsp83 (Xiao and Lis, 1988, Science 239: 1139-42)]. Peaks in Hsp26 and Hsp28 mRNA are correlated with peaks in ecdysteroid titres in mid-embryogenesis pupariation, and mid pupation (Thomas and Lengyel, 1986, Dev. Biol. 115: 434-38). # Hsp68 phenotype: The structural gene for the 68,000 dalton heat-shock protein (HSP68). molecular biology: The gene has been cloned and restriction mapped; it is represented but once in the genome (Holmgren, Livak, Morimoto, Freund, and Meselson, 1979, Cell 18: 1359- 70). Thermal stability tests indicates that there is about 15% sequence divergence between Hsp68 and Hsp70. The mRNA of Hsp68 is 2.1 kb in length; there are no introns in the genomic sequence. # Hsp70 phenotype: The structural genes that code for the 70,000 dalton heat-shock protein (HSP70), the most abundant of the heat- shock proteins. HSP70 returns to preshock levels more rapidly than other heat-shock proteins following return to 25 (DiDomenico, Bugaisky, and Lindquist, 1982, Proc. Nat. Acad. Sci. USA 79: 6181-85). The protein becomes concentrated in nuclei during heat shock; disperses to cytoplasm during recovery; returns to nucleus upon further heat shock (Velazquez and Lindquist, 1984, Cell 36: 655-62). Appears not to be expressed in the testis in response to heat-shock stimulation (Bonner, Parks, Parker-Thornberg, Mortin, and Pel- ham, 1984, Cell 37: 979-91). Deletion of either the 87A7 or the 87C1 sequences does not eliminate the HSP70 heat-shock response; simultaneous deletion of both sequences does elim- inate the HSP70 heat-shock response (Ish-Horowitz et al., 1979). molecular biology: mRNA for a 70 kilodalton heat-shock protein hybridizes to both 87A and 87C on the salivaries (Spradling, Pardue, and Penman, 1977, J. Mol. Biol. 109: 559-87). Several clones isolated from each region and sequences deter- mined. There are two copies of Hsp87A, and three copies of Hsp87C (Holmgren, Livak, Morimoto, Freund, and Meselson, 1979, Cell 18: 1359-70). Restriction maps of clones from the two regions differ slightly (Artavanis-Tsakonis, Steward, Gehring, Mirault, Goldschmidt-Clermont, Moran, and Tissieres, 1978, Cell 14: 921-29). Two copies of Hsp70 coding sequence at 87A arranged in divergent order with ATG codons separated by about 1700 nucleotide pairs (Goldschmidt-Clermont, 1980, Nucleic Acids Res. 8: 235-52). Sequence between the two determined (Mason, Torok, Kiss, Karch, and Udvardy, 1982, J. Mol. Biol. 156: 21-35). At 87 two copies separated by about 1000 nucleo- tides pairs are transcribed in the proximal to distal direc- tion; the third sequence, about 38,000 nucleotide pairs proxi- mal to the other two, is transcribed in the opposite direction (Ish-Horowitz and Pinchon, 1980, J. Mol. Biol. 142: 231-45; Mason et al., 1982). The proximal copy of Hsp70 at 87C sequenced by Ingolia, Craig, and McCarthy (1980, Cell 21: 669-79). Sequence 5 to Hsp70 coding sequences compared (Mason et al., 1982). Between the single proximal and two distal Hsp70 genes at 87C lie several repeated sequences designated (, |, and /. Hsp70 exhibits 48% homology with dnaK, a heat-shock gene in E. coli (Bardwell and Craig, 1984, Proc. Nat. Acad. Sci. USA 81: 848 52). 74% homology with the yeast Hsp70 genes, and 85% homology with mouse Hsp70 genes (Moran, Chauvin, Kennedy, Korri, Lowe, Nicholson, and Perry, 1983, Can. J. Biochem. Cell Biol. 61: 488-99). Activation of transcription on exposure to heat shock is carried out by upstream consensus elements or HSEs (see introduction) as indicated by deletion analyses of Hsp70 (Pelham, 1982, Cell 30: 517-28; McGarry and Lindquist, 1985, Cell 42: 903-11). Determination of sequence requirements by P-element germline transformation (Cohen and Meselson, 1984, Proc. Nat. Acad. Sci. USA 81: 5509-13). The HSE for Hsp70 was thought to be a 14-bp element, (Pelham, 1982); however, a very low level of heat-shock expression was obtained with two copies of the 14- bp HSE in flies carrying the Hsp70-lacZ hybrid gene. Recently, a HSE made up of contiguous arrays of inverted repeats of a 5-bp unit, -GAA-, has been proposed (Amin, Ananthan, and Voellmy, 1988, Mol. Cell Biol. 8: 3761-69; Xiao and Lis, 1988, Science 239: 1139-42; Perisic, Xiao, and Lis, 1989, Cell 59: 797-806); the Drosophila melanogaster Hsp70 gene has four arrays of three or four 5-bp units each (Per- isic, Xiao, and Lis, 1989). # Hsp83 phenotype: The structural gene for the 83,000 dalton heat-shock protein (HSP83). During development, the gene is expressed at high levels in the absence of heat shock in many tissues, especially ovaries where it apparently originates in nurse cells (Zimmerman, Petri, and Meselson, 1983, Cell 32: 1161- 70). During heat shock, however, the expression level is only raised several fold (Xiao and Lis, 1989, Mol. Cell Biol. 9: 1746-53). Deletion of sequences upstream from the coding region eliminates normal developmental expression and results in regulation of Hsp83 in a manner similar to that of Hsp70 which is activated only in response to heat shock. molecular biology: The sequence, which is unique, has been cloned, restriction mapped, and sequenced (Hackett and Lis, 1983, Nucleic Acids Res. 11: 7011-30; Blackman and Meselson, 1986, J. Mol. Biol. 188: 499-515). The mRNA is 2.6 kb in length; no introns found in genomic sequence. The expression of the gene during normal development (in the absence of heat shock) was thought to be due to the affinity of three overlap- ping, 14-bp heat shock consensus elements for a trans-acting heat shock factor (Xiao and Lis, 1986, Mol. Cell Biol. 6: 3200-06). Deletion mutants carrying the multiple HSEs, however, lost most of their developmental expression, but responded to heat shock like Hsp70. Recently Xiao and Lis (1989, Mol. Cell Biol. 9: 1746-53) have proposed that regula- tion of Hsp83 is the result of a single array of eight 5-bp units (-GAA). Upstream regions necessary for expression of ovarian development carry a 7-bp sequence CGTTTTG and multiple copies of the shorter sequence GTTTT (Xiao and Lis, 1989). A peak in Hsp83 mRNA is correlated with a peak in ecdysteroid titre in mid-embryogenesis, pupariation, and mid-pupation (Thomas and Lengyel, 1986, Dev. Biol. 115: 434-38). # Hsr93D: Heat-shock RNA at 93D location: 3-71 (based on cytological position with respect to e). synonym: hsrw. references: Bonner and Pardue, 1976, Cell 8: 43-50. Mohler and Pardue, 1984, Genetics 106: 249-65. Walldorf, Richter, Ryseck, Steller, Edstrom, Bautz, and Hovemann, 1984, EMBO J. 3: 2499-2505 Garbe and Pardue, 1986, Proc. Nat. Acad. Sci. USA 83: 1812- 16. Garbe, Bandena, Alfano, and Pardue, 1986, J. Biol. Chem. 261: 16889-94. Bandena, Garbe, Traverse, Lakhotia, and Pardue, 1989, J. Cell Biol. 108: 2017-28. Garbe, Bandena, and Pardue, 1989, Genetics 122: 403-15. Lakhotia, 1989, Genome 31: 677-803. phenotype: A sequence that responds to heat shock by generation of a large puff in polytene chromosomes. The 93D region tran- scribes mRNA that apparently is not translated. Hsr93D is active in almost all cells in Drosophila melanogaster; the activity is greatly increased by heat shock (Bonner and Par- due, 1976) and is induced independently by benzamide (Lakhotia and Mukherjee, 1970, DIS 45: 108). The inducibility of the locus is selectively repressed by a combination of heat shock with another inducer, by rearing larvae at 10, by heterozygous deficiency for 93D or by treating wild-type salivaries with beta-alanine (Lakhotia, 1989). The 93D heat shock mRNA is predominately polyA- in the cytoplasm, whereas nuclear tran- scripts are both polyA+ and polyA- (Lengyel, Randson, Grahm, and Pardue, 1980, Chromosoma 80: 237-52). Heat-shock response in homozygous deficiencies for Hsr93D is indistin- guishable from normal except for the absence of the 93D puff and transcripts. cytology: Placed between 93D4 and 93D9 by deficiency mapping. molecular biology: Transcribed region of the genome cloned and sequenced (Walldorf et al., 1984; Garbe and Pardue, 1986; Garbe et al., 1986 1989). Shown by TacqI digestion to comprise a 10-12 kilobase tandem array of 280 nucleotide repeat sequences. Transcripts produced following heat shock comple- mentary to TacqI repeat sequence but not to flanking sequences. There are three overlapping transcripts, all from the same start site. The largest transcript, w1, is limited to the nucleus and is composed of about 3 kb of unique regions followed by 7-17 kb of short tandem repeats (Bendena et al., 1989). The second transcript, w2, also nuclear, contains the first 2-3 kb of the unique region. The cytoplasmic tran- script, w3, has the same sequence as w2 minus an intron of about 700 bp (Garbe et al., 1986). All three transcripts are produced in nonstressed cells, but the transcript level is increased significantly when the cells are heat shocked. Drugs such as benzamide that increase puffing, lead to large increase in the w1 transcript. There are no long open reading frames (Garbe et al., 1989). Although Hsr93D does not encode any known heat-shock protein, there is some evidence that the cytoplasmic mRNA w3 contains a very small open reading frame (ORF w) that would encode 23 to 27 amino acids and is con- served in D. melanogaster, D. pseudoobscura, and D. hydei (Fini, Bendena, and Pardue, 1989, J. Cell Biol. 108: 2045-57; Garbe et al., 1989). # Hsr ( | location: 3-51 (based on cytological location). references: Lis, Prestidge, and Hogness, 1978, Cell 14: 901- 19. Livak, Freund, Schweber, Wensink, and Meselson, 1978, Proc. Nat. Acad. Sci. USA 75: 5613-17. Hackett and Lis, 1981, Proc. Nat. Acad. Sci. USA 78: 6196- 6200. phenotype: Repeated sequences that are transcribed in response to heat shock. Not translated. cytology: Localized to 87C1. molecular biology: A series of tandemly repeating units, each comprising an ( (0.49 kb) and a | (1.10 kb), located between the proximal two, divergently oriented, Hsp70 gene sequences in 87C. There are several tandem arrays separated by non- transcribed spacer regions. In some of the elements | is replaced by / (0.87 kb), which is homologous to sequences 5' to all five Hsp70 genes. # HsrW: see Hsr93D # hth: homothorax location: 3-48. origin: Induced with ethyl methanesulfonate. references: Jurgens, Wieschaus, Nusslein-Volhard, and Kluding, 1984, Wilhelm Roux's Arch. Dev. Biol. 193: 283-95 (fig.). phenotype: Homozygous lethal. Thoracic segments of embryo similar to one another; morphology of denticle bands inter- mediate between that of normal first and second thoracic seg- ments. cytology: Placed in 85E-86B by segmental aneuploids. # Hu: see AntpHu under ANTC # Huba: see Fs(3)Sz12 # Humeral patch: see Hup # humped: see hp # humpy: see hy # hunchback: see hb # hup: hold-up location: 2-44 (probably to the left of abo based on failure of 8 recombinants between da and hup to separate hup from abo). origin: Induced by ethyl methanesulfonate. references: Sandler, 1977, Genetics 86: 567-82. Lindsley, D.E., Goldstein, and Sandler, 1980, DIS 55: 84-85. phenotype: Nearly completely penetrant upheld wing. Homozy- gotes viable and semisterile in both sexes. Lethal in combi- nation with deficiency. Mortality of zygotes produced by hup mothers increased by the presence of a paternally inherited Y chromosome but not by the quantity of paternally derived X heterochromatin. Maternal effect at 25 more severe than at 19. Fertility also temperature sensitive; spermatids of sterile males show micronuclei and occasional double basal bodies and axonemes. cytology: Placed in 31F-32E based on inclusion in Df(2L)J39 = Df(2L)31A-B;32E but not Df(2L)J27 = Df(2L)31B-D;31F of Df(2L)Mdh-2J = Df(2L)30D-F;31F. other information: Complements abo, dal, and wd2. # Hup: Humeral patch location: 1-{20}. references: Merriam, Yamamoto, Stewart, Rahman, and Nicolau, unpublished. phenotype: A haplo-sensitive site on the X chromosome. Patch on either side of the thorax including the humeral bristles appears extended as a knobby outgrowth. cytology: Placed in 7C by segmental aneuploidy. # hv: heavy-vein location: 2-104.0. discoverer: Curry, 36l15. phenotype: Veins thick and knotty, especially at ends of crossveins; posterior crossvein oblique and may show break in middle; extra crossveins sometimes present. Wings broad, thick, dark, warped, divergent, and droopy. Eyes small and bulging. Posterior scutellars blunt, short, and crossed. Overlaps wild type at 25 but useful at 19. RK2. #*Hv: Hooked-veins location: 1-66. discoverer: Tanaka, 35a4. references: 1935, DIS 4: 16. 1936, DIS 5: 8. 1937, DIS 8: 11. phenotype: Heterozygous female shows small branches from poste- rior crossvein and L5. Eyes small and rough. Homozygous female lethal. RK3A. cytology: Associated with In(1)Hv. # Hw: see ASC # Hx: Hexaptera location: 2- (not located). origin: Spontaneous. discoverer: Herskowitz, 47j. references: 1949, Genetics 34: 10-25 (fig.). phenotype: Expression same in Hx/+ and Hx/Hx, varies from absence of a detectable difference from normal through various intermediate types to presence of large appendage on prothorax. Entire abnormal structure may remain beneath exoskeleton. Appendage varies from small amorphous mass to highly differentiated wing. May also produce haltere- and leg-like appendages. Penetrance same in homozygote and heterozygote; prothorax to mesothorax transformation, enhanced by crowding and by high temperature (at 20, male 1.5 and female 3.3%; at 25, male 6.5 and female 24.2%); and affected by genotype, e.g., suppressed by In(2L+2R)Cy and by In(2LR)bwV1. RK3. # hy: humpy location: 2-93.3. origin: Spontaneous. discoverer: Bridges, 18j22. references: 1937, Cytologia (Tokyo), Fujii Jub., Vol. 2: 745- 55. phenotype: Thorax strongly ridged with commas anteriorly and two pairs of vortices. Wings obliquely truncated to one-half normal length. An irregular contraction of larval muscles at time of pupation (Waddington, 1941, Proc. Zool. Soc. London Ser. A 111: 181-88). Viability low and erratic. Both sexes highly infertile. RK2. cytology: Placed in region 57 on basis of its being to the right of In(2R)NS = In(2R)52A2-B1;56F9-13 and to the left of Df(2R)M-1 = Df(2R)57F11-58A1;58F8-59A1 (Bridges, 1937). # hybrid male rescue: see hmr # Hydroxy acid dehydrogenase: see Had # Hydroxphenyl buten-1: see Hpb hy: humpy Edith M. Wallace, unpublished. # hyperantenna: see hpa # Hyperkinetic: see Hk # hypoA: hypoactive-A (J.C. Hall) location: 1-1.0. origin: Induced by ethyl methanesulfonate. references: Homyk and Sheppard, 1977, Genetics 87: 95-104. phenotype: Inactive; difficult to arouse for flight; runs and climbs slowly; jumps and flies abnormally short distances; slow optomotor response; debilitated after mechanical stress. # hypoB: see iav (in addendum) # hypoC (J.C. Hall) location: 1-44.3. origin: Induced by ethyl methanesulfonate. references: Homyk and Sheppard, 1977, Genetics 87: 95-104. Homyk, 1977, Genetics 87: 105-28. O'Dell and Burnet, 1988, Heredity 61: 199-207. O'Dell, Burnet and Jallon, 1989, Heredity 62: 373-81. phenotype: Relatively inactive (Homyk and Sheppard, 1977); dif- ficult to arouse for flight; flies abnormally slow (hovers and fixates on object while flying); runs and climbs slowly; slow optomotor response. Jumping ability very poor (O'Dell and Burnet, 1988). Mosaic analysis (Homyk, 1977) suggests primary defect could be in central nervous system or in muscles. In open field activity chamber tests (O'Dell and Burnet, 1988), moves as much as wild-type initially (0-10 minutes) but becomes less active later (10-20 minutes); both speed and amount of movement affected (e.g. in aging tests, both metrics increase in parallel from day 1 to 16 of adulthood, whereas wild types show near-maximal levels of activity as young adults, with slow decline during subsequent one month). When homozygous in females, causes reduced mating propensity and extended courtship durations (O'Dell et al., 1989). alleles: hypoC1, hypoC2. # hypoD: see slrp # hypoE (J.C. Hall) location: 1-39.2. origin: Induced by ethyl methanesulfonate. references: Homyk, Szidonya, and Suzuki, 1980, Molec. Gen. Genet. 177: 553-65. O'Dell and Burnet, 1988, Heredity 61: 199-207. O'Dell, Burnet and Jallon, 1989, Heredity 62: 373-81. phenotype: Subnormal activity (Homyk et al., 1980); requires extensive agitation to induce movements and becomes inactive more quickly than normal when agitation ceases; males inactive in courtship. Jumping ability very poor (O'Dell and Burnet, 1988). In open field chamber tests (O'Dell and Burnet, 1988), speed of locomotion (number of squares entered/unit time) reduced but not the amount (proportion of time spend moving); amount of speed changes in wild-type-like manner with advanc- ing adult age (cf. hypoC) When hypoE homozygous in females, their receptivity to male courtship and mating attempts is essentially the same as for wild-type females (O'Dell et al., 1989). other information: Complements the closely linked comt muta- tions. # hypoF: see rdgB # hypoG (J.C. Hall) location: 1-50.8. references: Homyk, Szidonya, and Suzuki, 1980, Molec. Gen. Genet. 177: 553-65. phenotype: Subnormal activity, similar to that caused by hypoE, except hypoG more abnormal, including decreasing and rela- tively quick cessation of wing beats in flight plus weak opto- motor response.