By Gustavo Maroni
Drosophila, the typical fruit fly, is the main widely studied of all organisms from the perspective of genetics and cytology. This atlas summarizes what's recognized in regards to the nearly a hundred Drosophila genes for which the total nucleotide series is understood. each one access features a description of the gene's molecular association and expression, the entire nucleotide and amino acid sequences, maps of fascinating buildings, highlights of sensible beneficial properties and promoter regulatory areas, and chosen references to the first literature. A separate element of the atlas considers diversified facets of gene association as they happen within the Drosophila genome. subject matters coated comprise dimension correlations between numerous genetic components, splicing signs, translation initiation indications, and codon bias. The paintings represents a brand new milestone in summarizing present details and making it simply available to geneticists and biologists.
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Extra resources for An Atlas of Drosophila Genes: Sequences and Molecular Features
O. and Tobin, S. L. (1989). Alternative 5C actin transcripts are localized in different patterns during Drosophila embryogenesis. Dev. Biol. 131:345-355. -T. and Keller, E. B. (1990a). Regulatory elements mediating transcription from the Drosophila melanogaster Actin 5C proximal promoter. Mol. Cell. Biol. 10:206-216. -T. and Keller, E. B. (1990b). Positive and negative regulatory elements mediating transcription from the Drosophila melanogaster Actin 5C distal promoter. Mol. Cell. Biol. 10:6172-6180.
Because most of the coding sequence was determined from a cDNA, the presence of other small introns cannot be ruled out (Act42A sequence) (Fyrberg et al. 1981; Couderc et al. 1987). Developmental Pattern During embryonic development, Act42A transcription follows a pattern similar to that of ActSC. The accumulation of transcripts is greatest in the midgut, central nervous system and gonads (Tobin et al. 1990). Act42A is expressed in Act42A SEQUENCE (opposite). Mostly from Canton S. Accession, K00670, K00671 (DROACT2A), X05176 (DROACT42A).
4 kD; the polypeptide is 255 amino acids long with Acetyl-Ser at the amino terminus. There are two common allozymes, Slow (S) and Fast (F), that differ in electrophoretic mobility due to a threonine/lysine substitution at position 192. Unlike the ADH of other species, Drosophila ADH does not use Zn as a cofactor. Amino acid sequence comparisons reveal significant differences between Drosophila ADH on one hand and ADH from yeast or horse liver on the other (the latter two being quite similar); these observations suggest that the Drosophila protein is not homologous to other ADHs (Thatcher 1980; Benyajati et al.