Abstract
We present the complete nucleotide sequence of a Drosophila alpha-amylase gene and its flanking regions, as determined by cDNA and genomic sequence analysis. This gene, unlike its mammalian counterparts, contains no introns. Nevertheless the insect and mammalian genes share extensive nucleotide similarity and the insect protein contains the four amino acid sequence blocks common to all alpha-amylases. In Drosophila melanogaster, there are two closely-linked copies of the alpha-amylase gene and they are divergently transcribed. In the 5'-regions of the two gene-copies we find high sequence divergence, yet the typical eukaryotic gene expression motifs have been maintained. The 5'-terminus of the alpha-amylase mRNA, as determined by primer extension analysis, maps to a characteristic Drosophila sequence motif. Additional conserved elements upstream of both genes may also be involved in amylase gene expression which is known to be under complex controls that include glucose repression.
Full text
PDF












Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Benkel B. F., Hickey D. A. Glucose Repression of Amylase Gene Expression in DROSOPHILA MELANOGASTER. Genetics. 1986 Sep;114(1):137–144. doi: 10.1093/genetics/114.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Birnstiel M. L., Busslinger M., Strub K. Transcription termination and 3' processing: the end is in site! Cell. 1985 Jun;41(2):349–359. doi: 10.1016/s0092-8674(85)80007-6. [DOI] [PubMed] [Google Scholar]
- Doane W. W., Treat-Clemons L. G., Gemmill R. M., Levy J. N., Hawley S. A., Buchberg A. M., Paigen K. Genetic mechanism for tissue-specific control of alpha-amylase expression in Drosophila melanogaster. Isozymes Curr Top Biol Med Res. 1983;9:63–90. [PubMed] [Google Scholar]
- Gemmill R. M., Schwartz P. E., Doane W. W. Structural organization of the Amy locus in seven strains of Drosophila melanogaster. Nucleic Acids Res. 1986 Jul 11;14(13):5337–5352. doi: 10.1093/nar/14.13.5337. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Guarente L., Lalonde B., Gifford P., Alani E. Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiae. Cell. 1984 Feb;36(2):503–511. doi: 10.1016/0092-8674(84)90243-5. [DOI] [PubMed] [Google Scholar]
- Hagenbüchle O., Bovey R., Young R. A. Tissue-specific expression of mouse-alpha-amylase genes: nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland. Cell. 1980 Aug;21(1):179–187. doi: 10.1016/0092-8674(80)90125-7. [DOI] [PubMed] [Google Scholar]
- Henikoff S., Keene M. A., Fechtel K., Fristrom J. W. Gene within a gene: nested Drosophila genes encode unrelated proteins on opposite DNA strands. Cell. 1986 Jan 17;44(1):33–42. doi: 10.1016/0092-8674(86)90482-4. [DOI] [PubMed] [Google Scholar]
- Hultmark D., Klemenz R., Gehring W. J. Translational and transcriptional control elements in the untranslated leader of the heat-shock gene hsp22. Cell. 1986 Feb 14;44(3):429–438. doi: 10.1016/0092-8674(86)90464-2. [DOI] [PubMed] [Google Scholar]
- Karn R. C., Petersen T. E., Hjorth J. P., Nieles J. T., Roepstorff P. Characterization of the amino termini of mouse salivary and pancreatic amylases. FEBS Lett. 1981 Apr 20;126(2):293–296. doi: 10.1016/0014-5793(81)80264-5. [DOI] [PubMed] [Google Scholar]
- Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984 Jan 25;12(2):857–872. doi: 10.1093/nar/12.2.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kreitman M. Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster. Nature. 1983 Aug 4;304(5925):412–417. doi: 10.1038/304412a0. [DOI] [PubMed] [Google Scholar]
- Levy J. N., Gemmill R. M., Doane W. W. Molecular cloning of alpha-amylase genes from Drosophila melanogaster. II. Clone organization and verification. Genetics. 1985 Jun;110(2):313–324. doi: 10.1093/genetics/110.2.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mackay R. M., Baird S., Dove M. J., Erratt J. A., Gines M., Moranelli F., Nasim A., Willick G. E., Yaguchi M., Seligy V. L. Glucanase gene diversity in prokaryotic and eukaryotic organisms. Biosystems. 1985;18(3-4):279–292. doi: 10.1016/0303-2647(85)90028-0. [DOI] [PubMed] [Google Scholar]
- Matsuura Y., Kusunoki M., Harada W., Kakudo M. Structure and possible catalytic residues of Taka-amylase A. J Biochem. 1984 Mar;95(3):697–702. doi: 10.1093/oxfordjournals.jbchem.a134659. [DOI] [PubMed] [Google Scholar]
- Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
- Moore G. W., Goodman M., Callahan C., Holmquist R., Moise H. Stochastic versus augmented maximum parsimony method for estimating superimposed mutations in the divergent evolution of protein sequences. Methods tested on cytochrome c amino acid sequences. J Mol Biol. 1976 Jul 25;105(1):15–37. doi: 10.1016/0022-2836(76)90193-5. [DOI] [PubMed] [Google Scholar]
- Nishide T., Emi M., Nakamura Y., Matsubara K. Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected]. Gene. 1984 May;28(2):263–270. doi: 10.1016/0378-1119(84)90265-8. [DOI] [PubMed] [Google Scholar]
- Nussinov R. Sequence signals which may be required for efficient formation of mRNA 3' termini. Nucleic Acids Res. 1986 Apr 25;14(8):3557–3571. doi: 10.1093/nar/14.8.3557. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Connell P. O., Rosbash M. Sequence, structure, and codon preference of the Drosophila ribosomal protein 49 gene. Nucleic Acids Res. 1984 Jul 11;12(13):5495–5513. doi: 10.1093/nar/12.13.5495. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Queen C., Korn L. J. A comprehensive sequence analysis program for the IBM personal computer. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 2):581–599. doi: 10.1093/nar/12.1part2.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rogers J. C. Conserved amino acid sequence domains in alpha-amylases from plants, mammals, and bacteria. Biochem Biophys Res Commun. 1985 Apr 16;128(1):470–476. doi: 10.1016/0006-291x(85)91702-4. [DOI] [PubMed] [Google Scholar]
- Rogers J. C., Milliman C. Isolation and sequence analysis of a barley alpha-amylase cDNA clone. J Biol Chem. 1983 Jul 10;258(13):8169–8174. [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shuster J., Yu J., Cox D., Chan R. V., Smith M., Young E. ADR1-mediated regulation of ADH2 requires an inverted repeat sequence. Mol Cell Biol. 1986 Jun;6(6):1894–1902. doi: 10.1128/mcb.6.6.1894. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Singh R. S., Hickey D. A., David J. Genetic Differentiation between Geographically Distant Populations of DROSOPHILA MELANOGASTER. Genetics. 1982 Jun;101(2):235–256. doi: 10.1093/genetics/101.2.235. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takkinen K., Pettersson R. F., Kalkkinen N., Palva I., Söderlund H., Käriäinen L. Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J Biol Chem. 1983 Jan 25;258(2):1007–1013. [PubMed] [Google Scholar]
- Yang M., Galizzi A., Henner D. Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucleic Acids Res. 1983 Jan 25;11(2):237–249. doi: 10.1093/nar/11.2.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Young E. T., Pilgrim D. Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol Cell Biol. 1985 Nov;5(11):3024–3034. doi: 10.1128/mcb.5.11.3024. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zuker C. S., Cowman A. F., Rubin G. M. Isolation and structure of a rhodopsin gene from D. melanogaster. Cell. 1985 Apr;40(4):851–858. doi: 10.1016/0092-8674(85)90344-7. [DOI] [PubMed] [Google Scholar]
- de Banzie J. S., Sinclair L., Lis J. T. Expression of the major heat shock gene of Drosophila melanogaster in Saccharomyces cerevisiae. Nucleic Acids Res. 1986 Apr 25;14(8):3587–3601. doi: 10.1093/nar/14.8.3587. [DOI] [PMC free article] [PubMed] [Google Scholar]