The alpha-amylase gene inDrosophila mdanogaster: nucleotide sequence, gene structure and expression motifs
- 1 January 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 14 (21), 8399-8411
- https://doi.org/10.1093/nar/14.21.8399
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.Keywords
This publication has 27 references indexed in Scilit:
- Translational and transcriptional control elements in the untranslated leader of the heat-shock gene hsp22Cell, 1986
- Gene within a gene: Nested Drosophila genes encode unrelated proteins on opposite DNA strandsCell, 1986
- Transcription termination and 3′ processing: the end is in site!Cell, 1985
- Conserved amino acid sequence domains in alpha-amylases from plants, mammals, and bacteriaBiochemical and Biophysical Research Communications, 1985
- Isolation and structure of a rhodopsin gene from D. melanogasterCell, 1985
- Sequences of cDNAs for human salivary and pancreatic α-amylasesGene, 1984
- Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiaeCell, 1984
- Characterization of the amino termini of mouse salivary and pancreatic amylasesFEBS Letters, 1981
- Tissue-specific expression of mouse α-amylase genes: Nucleotide sequence of isoenzyme mRNAs from pancreas and salivary glandCell, 1980
- Stochastic versus augmented maximum parsimony method for estimating superimposed mutations in the divergent evolution of protein sequences. Methods tested on cytochrome c amino acid sequencesJournal of Molecular Biology, 1976