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Genetic localization of a regulatory site necessary for the production of the glue protein P5 in Drosophila melanogaster

Published online by Cambridge University Press:  14 April 2009

Deborah K. Hoshizaki ,
Bonnie M. Dlott ,
Geoffrey L. Joslyn  and
Steven K. Beckendorf
Deborah K. Hoshizaki
Affiliation:
Departments of Molecular Biology and Genetics, University of California, Berkeley, California 94720
Bonnie M. Dlott
Affiliation:
Departments of Molecular Biology and Genetics, University of California, Berkeley, California 94720
Geoffrey L. Joslyn
Affiliation:
Departments of Molecular Biology and Genetics, University of California, Berkeley, California 94720
Steven K. Beckendorf
Affiliation:
Departments of Molecular Biology and Genetics, University of California, Berkeley, California 94720
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Summary

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The glue proteins are products of a developmentally regulated gene family. These genes are transcriptionally active during the third larval instar and code for the major protein products of salivary glands. The activity of several of the genes can be visualized as intermoult puffs in the polytene salivary gland chromosomes. The amount of one of these proteins, P5, varies widely among wild-type strains. We have used biochemical and genetic methods to investigate the source of this variation. The results of in vitro translation of salivary gland RNA suggest that the variation occurs pretranslationally. Genetic mapping experiments showed that sites on several chromosomes can modulate the amount of P5, but that one site on the third chromosome determines the absence and presence of this protein. We have mapped this glue protein gene, called GP5, to the interval between bx (3–58·8) and sr (3–62·0) which also includes the intermoult puff at 90BC. We discuss the relationship between P5 and the glue protein gene Sgs-5 which is also located at 90BC.

Type
Research Article
Information
Genetics Research , Volume 49 , Issue 2 , April 1987 , pp. 111 - 119
Copyright
Copyright © Cambridge University Press 1987

References

Akam, M. E., Roberts, D. B., Richards, G. P. & Ashburner, M. (1978). Drosophila: the genetics of two major larval proteins. Cell 13, 215–225.CrossRefGoogle ScholarPubMed
Beckendorf, S. K. & Kafatos, F. C. (1976). Differentiation in the salivary glands of Drosophila melanogaster: characterization of the glue proteins and their developmental appearance. Cell 9, 365–373.CrossRefGoogle ScholarPubMed
Bonner, W. M. & Laskey, R. A. (1974). A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. European Journal of Biochemistry 46, 83–88.CrossRefGoogle ScholarPubMed
Cohen, L. H. & Gotchel, B. V. (1971). Histones of polytene and nonpolytene nuclei of Drosophila melanogaster. Journal of Biological Chemistry 246, 1841–1848.Google Scholar
Corces, V., Holmgren, R., Freund, R., Morimoto, R. & Meselson, M. (1980). Four heat shock proteins of Drosophila melanogaster coded within a 12-kilobase region in chromosome subdivision 67B. Proceedings of the National Academy of Sciences USA 77, 5390–5393.Google Scholar
Efstratiadis, A. & Kafatos, F. (1976). Thechorion of insects: techniques and perspectives. In Methods in Molecular Biology, vol. 8. (ed. Last, J.), New York: Marcel Dekker.Google Scholar
Guild, G. M. & Shore, E. M. (1984). Larval salivary gland secretion proteins in Drosophila. Identification and characterization of the Sgs-5 structural gene. Journal of Molecular Biology 179, 289–314.CrossRefGoogle ScholarPubMed
Ish-Horowicz, D., Pinchin, S. M., Schedl, P., Artavanis-Tsakonas, S. & Mirault, M. -E. (1979). Genetic and molecular analysis of 87A7 and 87C1 heat-inducible loci of D. melanogaster. Cell 18, 1351–1358.CrossRefGoogle ScholarPubMed
Kodani, M. (1948). The protein of the salivary gland secretion in Drosophila. Proceedings of the National Academy of Sciences USA 34, 131–135.CrossRefGoogle ScholarPubMed
Korge, G. (1975). Chromosome puff activity and protein synthesis in larval salivary glands of Drosophila melanogaster. Proceedings of the National Academy of Sciences USA 72, 4550–4554.CrossRefGoogle ScholarPubMed
Korge, G. (1977). Larval saliva in Drosophila melanogaster: production, composition and relationship to chromosome puffs. Developmental Biology 58, 339–355.Google Scholar
Korge, G. (1981). Genetic analysis of the larval secretion gene Sgs-4 and its regulatory chromosome site in Drosophila melanogaster. Chromosoma 84, 373–390.Google Scholar
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680–685.Google Scholar
Laskey, R. A. & Mills, A. D. (1975). Quantitative film detection of H3 and C14 in polyacrylamide gels by fluorography. European Journal of Biochemistry 56, 335–341.CrossRefGoogle Scholar
Lindsley, D. L. & Grell, E. H. (1968). Genetic variations of Drosophila melanogaster. Carnegie Institution of Washington, Publication No. 627.Google Scholar
McGinnis, W., Shermoen, A. W., Heemskerk, J. & Beckendorf, S. K. (1983 a). DNA sequence changes in an upstream DNAse-1 hypersensitive region are correlated with reduced gene expression. Proceedings of the National Academy of Sciences USA 80, 1063–1067.Google Scholar
McGinnis, W., Shermoen, A. W., & Beckendorf, S. K. (1983 b). A transposable element inserted just 5′ to a Drosophila glue protein gene alters gene expression and chromatin structure. Cell 34, 75–84.Google Scholar
Meyerowitz, E. M. & Hogness, D. S. (1982). Molecular organization of a Drosophila puff site that responds to ecdysone. Cell 28, 165–176.CrossRefGoogle ScholarPubMed
Muskavitch, M. A. T. & Hogness, D. S. (1980). Molecular analysis of a gene in a developmentally regulated puff of Drosophila melanogaster. Proceedings of the National Academy of Sciences USA 77, 7362–7366.CrossRefGoogle Scholar
Muskavitch, M. A. T. & Hogness, D. S. (1982). An expandable gene that encodes a Drosophila glue protein is not expressed in variants lacking remote upstream sequences. Cell 29: 1041–1051.CrossRefGoogle Scholar
Palmiter, R. D. (1974). Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undegraded polysomes and messenger ribonucleic acid. Biochemistry 13, 3606–3615.Google Scholar
Restifo, L. L. & Guild, G. M. (1986). An ecdysone responsive puff site in Drosophila contains a cluster of seven differentially regulated genes. Journal of Molecular Biology (in press).Google Scholar
Roberts, B. E. & Paterson, B. M. (1973). Efficient translation of Tobacco Mosaic virus RNA and rabbit globin 9S RNA in a cell free system from commercial wheat germ. Proceedings of the National Academy of Sciences USA 70, 2330–2334.Google Scholar
Velissariou, V. & Ashburner, M. (1980). The secretory proteins of the larval salivary gland of Drosophila melanogaster. Cytological correlation of a protein and a puff. Chromosoma (Berlin) 77, 13–27.Google Scholar
Velissariou, V. & Ashburner, M. (1981). Cytogenetic and genetic mapping of a salivary gland secretion protein in Drosophila melanogaster. Chromosoma (Berlin) 84, 173–185.Google Scholar
Williams, D. E. & Reisfeld, R. A. (1964). Disc electrophoresis in poly-acrylamide gels: extension to new conditions of pH and buffers. Annals of the New York Academy of Science 121, 373–381.Google Scholar
Wolfner, M. F. (1980). Ecdysone-responsive genes of the salivary glands of Drosophila melanogaster. Ph.D. Thesis, Stanford University, Stanford, CA.Google Scholar
Zweidler, A. & Cohen, L. H. (1971). Large scale isolation and fractionation of organs of Drosophila melanogaster larvae. Journal of Cell Biology 51, 240–248.Google Scholar