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一个编码252个氨基酸的非肌肉原肌球蛋白同工型的果蝇cDNA克隆的鉴定。

Characterization of a Drosophila cDNA clone that encodes a 252-amino acid non-muscle tropomyosin isoform.

作者信息

Hanke P D, Lepinske H M, Storti R V

机构信息

Department of Biological Chemistry, University of Illinois College of Medicine, Chicago 60612.

出版信息

J Biol Chem. 1987 Dec 25;262(36):17370-3.

PMID:3693358
Abstract

We report here the isolation and DNA sequence of a cDNA clone encoding a 252-amino acid non-muscle or cytoskeletal tropomyosin (cTm) isoform from Drosophila. The Drosophila cTm shows considerable homology with vertebrate cTm throughout the middle portion of the molecule. The amino-terminal end of the molecule, however, shows less homology and contains five more amino acids than the equine platelet and human tropomyosins. There is also a proline at position 6 in the Drosophila protein. The carboxyl-terminal 27 amino acids also show little homology with vertebrate non-muscle tropomyosins. This is a region of the molecule that shows considerably diversity among other Drosophila tropomyosins and vertebrate tropomyosins. A comparison of the DNA sequence of the cTm cDNA and a previously reported muscle tropomyosin II cDNA sequence shows regions of identical DNA sequence alternating with regions of nonidentical sequence, suggesting that both mRNAs are produced by alternate splicing of the same gene.

摘要

我们在此报告从果蝇中分离出的一个编码252个氨基酸的非肌肉或细胞骨架原肌球蛋白(cTm)同工型的cDNA克隆及其DNA序列。果蝇cTm在分子的中间部分与脊椎动物cTm具有相当高的同源性。然而,该分子的氨基末端同源性较低,比马血小板和人原肌球蛋白多五个氨基酸。果蝇蛋白的第6位还有一个脯氨酸。羧基末端的27个氨基酸与脊椎动物非肌肉原肌球蛋白的同源性也很低。这是该分子的一个区域,在其他果蝇原肌球蛋白和脊椎动物原肌球蛋白中表现出相当大的多样性。cTm cDNA的DNA序列与先前报道的肌肉原肌球蛋白II cDNA序列的比较显示,相同DNA序列区域与不同序列区域交替出现,这表明这两种mRNA都是由同一基因的可变剪接产生的。

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