嗜热四膜虫肌动蛋白单体结合蛋白的一级结构。

The primary structure of Tetrahymena profilin.

作者信息

Edamatsu M, Hirono M, Takemasa T, Watanabe Y

机构信息

Institute of Biological Sciences, University of Tsukuba, Japan.

出版信息

Biochem Biophys Res Commun. 1991 Mar 15;175(2):543-50. doi: 10.1016/0006-291x(91)91599-8.

DOI:10.1016/0006-291x(91)91599-8

PMID:1902095

Abstract

The cDNA of Tetrahymena profilin was cloned and sequenced. The deduced product has a molecular mass of 16,785 Da which is the largest among profilins known so far. Tetrahymena profilin shows higher homologies with lower eukaryotic profilins than with mammalian profilins. Although the homologies with mammalian and lower eukaryotic profilins are only 20-29% which is the lowest one among lower eukaryotic profilins, the N- and C-terminal regions of Tetrahymena profilin are considerably conserved as those in other profilins, suggesting that these regions are responsible for the essential properties common to profilins.

摘要

嗜热四膜虫肌动蛋白单体结合蛋白的互补DNA（cDNA）被克隆并测序。推导得出的产物分子量为16,785道尔顿，是迄今为止已知的肌动蛋白单体结合蛋白中最大的。与哺乳动物的肌动蛋白单体结合蛋白相比，嗜热四膜虫肌动蛋白单体结合蛋白与低等真核生物的肌动蛋白单体结合蛋白具有更高的同源性。尽管与哺乳动物和低等真核生物的肌动蛋白单体结合蛋白的同源性仅为20%-29%，这在低等真核生物的肌动蛋白单体结合蛋白中是最低的，但嗜热四膜虫肌动蛋白单体结合蛋白的N端和C端区域与其他肌动蛋白单体结合蛋白的相应区域相当保守，这表明这些区域决定了肌动蛋白单体结合蛋白共有的基本特性。