Abstract
The primary base sequence of the protein coding regions of the four small heat shock genes of Drosophila melanogaster present at cytological locus 67B has been determined. A single open reading frame large enough to encode a small heat shock protein is found for each gene. The molecular weights of the predicted proteins are in good agreement with experimentally determined values obtained from gel electrophoresis. The predicted amino acid sequences of the four small heat shock genes show striking homologies over approximately 50% of their lengths. This region of extensive homology extends from about amino acid 85 to amino acid 195 out of a total of approximately 200 amino acids. Comparison of the predicted sequence with the known sequences of other proteins revealed a remarkable similarity between this region of homology and the corresponding region of mammalian alpha-crystallin. The possible functional significance of this structural similarity is discussed.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Arrigo A. P., Fakan S., Tissières A. Localization of the heat shock-induced proteins in Drosophila melanogaster tissue culture cells. Dev Biol. 1980 Jul;78(1):86–103. doi: 10.1016/0012-1606(80)90320-6. [DOI] [PubMed] [Google Scholar]
- Ashburner M., Bonner J. J. The induction of gene activity in drosophilia by heat shock. Cell. 1979 Jun;17(2):241–254. doi: 10.1016/0092-8674(79)90150-8. [DOI] [PubMed] [Google Scholar]
- Bloemendal H., Berns T., Zweers A., Hoenders H., Benedetti E. L. The state of aggregation of -crystallin detected after large-scale preparation by zonal centrifugation. Eur J Biochem. 1972 Jan 21;24(3):401–406. doi: 10.1111/j.1432-1033.1972.tb19699.x. [DOI] [PubMed] [Google Scholar]
- Bloemendal H. The vertebrate eye lens. Science. 1977 Jul 8;197(4299):127–138. doi: 10.1126/science.877544. [DOI] [PubMed] [Google Scholar]
- Corces V., Holmgren R., Freund R., Morimoto R., Meselson M. Four heat shock proteins of Drosophila melanogaster coded within a 12-kilobase region in chromosome subdivision 67B. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5390–5393. doi: 10.1073/pnas.77.9.5390. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Craig E. A., McCarthy B. J. Four Drosophila heat shock genes at 67B: characterization of recombinant plasmids. Nucleic Acids Res. 1980 Oct 10;8(19):4441–4457. doi: 10.1093/nar/8.19.4441. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Craig E. A., McCarthy B. J., Wadsworth S. C. Sequence organization of two recombinant plasmids containing genes for the major heat shock-induced protein of D. melanogaster. Cell. 1979 Mar;16(3):575–588. doi: 10.1016/0092-8674(79)90031-x. [DOI] [PubMed] [Google Scholar]
- Holmgren R., Livak K., Morimoto R., Freund R., Meselson M. Studies of cloned sequences from four Drosophila heat shock loci. Cell. 1979 Dec;18(4):1359–1370. doi: 10.1016/0092-8674(79)90246-0. [DOI] [PubMed] [Google Scholar]
- Ingolia T. D., Craig E. A., McCarthy B. J. Sequence of three copies of the gene for the major Drosophila heat shock induced protein and their flanking regions. Cell. 1980 Oct;21(3):669–679. doi: 10.1016/0092-8674(80)90430-4. [DOI] [PubMed] [Google Scholar]
- Ingolia T. D., Craig E. A. Primary sequence of the 5' flanking regions of the Drosophila heat shock genes in chromosome subdivision 67B. Nucleic Acids Res. 1981 Apr 10;9(7):1627–1642. doi: 10.1093/nar/9.7.1627. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kelley P. M., Schlesinger M. J. The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts. Cell. 1978 Dec;15(4):1277–1286. doi: 10.1016/0092-8674(78)90053-3. [DOI] [PubMed] [Google Scholar]
- Loomis W. F., Wheeler S. Heat shock response of Dictyostelium. Dev Biol. 1980 Oct;79(2):399–408. doi: 10.1016/0012-1606(80)90125-6. [DOI] [PubMed] [Google Scholar]
- Maxam A. M., Gilbert W. A new method for sequencing DNA. Proc Natl Acad Sci U S A. 1977 Feb;74(2):560–564. doi: 10.1073/pnas.74.2.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McAlister L., Finkelstein D. B. Alterations in translatable ribonucleic acid after heat shock of Saccharomyces cerevisiae. J Bacteriol. 1980 Aug;143(2):603–612. doi: 10.1128/jb.143.2.603-612.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miller M. J., Xuong N. H., Geiduschek E. P. A response of protein synthesis to temperature shift in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5222–5225. doi: 10.1073/pnas.76.10.5222. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mirault M. E., Goldschmidt-Clermont M., Moran L., Arrigo A. P., Tissières A. The effect of heat shock on gene expression in Drosophila melanogaster. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 2):819–827. doi: 10.1101/sqb.1978.042.01.082. [DOI] [PubMed] [Google Scholar]
- Oppermann H., Levinson W., Bishop J. M. A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein. Proc Natl Acad Sci U S A. 1981 Feb;78(2):1067–1071. doi: 10.1073/pnas.78.2.1067. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schoenmakers J. G., Bloemendal H. Subunits of alpha-crystallin from adult and embryonic cattle lens. Nature. 1968 Nov 23;220(5169):790–791. doi: 10.1038/220790a0. [DOI] [PubMed] [Google Scholar]
- Sinibaldi R. M., Morris P. W. Putative function of Drosophila melanogaster heat shock proteins in the nucleoskeleton. J Biol Chem. 1981 Nov 10;256(21):10735–10738. [PubMed] [Google Scholar]
- Storti R. V., Scott M. P., Rich A., Pardue M. L. Translational control of protein synthesis in response to heat shock in D. melanogaster cells. Cell. 1980 Dec;22(3):825–834. doi: 10.1016/0092-8674(80)90559-0. [DOI] [PubMed] [Google Scholar]
- Talaat M., Hamdy H., el-Bagoury I. M., Abdel-Rahman Y. M., Makarem F., el-Shewy T. M. The effect of short- and long-acting barbiturates on the oxygen uptake of the intact lens and its homogenate. Exp Eye Res. 1974 Apr;18(4):381–382. doi: 10.1016/0014-4835(74)90115-8. [DOI] [PubMed] [Google Scholar]
- Van Der Ouderaa F. J., De Jong W. W., Hilderink A., Bloemendal H. The amino-acids sequence of the alphaB2 chain of bovine alpha-crystallin. Eur J Biochem. 1974 Nov 1;49(1):157–168. doi: 10.1111/j.1432-1033.1974.tb03821.x. [DOI] [PubMed] [Google Scholar]
- Velazquez J. M., DiDomenico B. J., Lindquist S. Intracellular localization of heat shock proteins in Drosophila. Cell. 1980 Jul;20(3):679–689. doi: 10.1016/0092-8674(80)90314-1. [DOI] [PubMed] [Google Scholar]
- Voellmy R., Goldschmidt-Clermont M., Southgate R., Tissières A., Levis R., Gehring W. A DNA segment isolated from chromosomal site 67B in D. melanogaster contains four closely linked heat-shock genes. Cell. 1981 Jan;23(1):261–270. doi: 10.1016/0092-8674(81)90290-7. [DOI] [PubMed] [Google Scholar]
- Wadsworth S. C., Craig E. A., McCarthy B. J. Genes for three Drosophila heat-shock-induced proteins at a single locus. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2134–2137. doi: 10.1073/pnas.77.4.2134. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wang C., Gomer R. H., Lazarides E. Heat shock proteins are methylated in avian and mammalian cells. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3531–3535. doi: 10.1073/pnas.78.6.3531. [DOI] [PMC free article] [PubMed] [Google Scholar]
- van der Ouderaa F. J., de Jong W. W., Bloemendal H. The amino-acid sequence of the alphaA2 chain of bovine alpha-crystallin. Eur J Biochem. 1973 Nov 1;39(1):207–222. doi: 10.1111/j.1432-1033.1973.tb03119.x. [DOI] [PubMed] [Google Scholar]