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盘基网柄菌的肌动蛋白交联蛋白EF-1a具有独特的结合规则,可形成方形排列的束状结构。

Actin crosslinking protein EF-1a of Dictyostelium discoideum has a unique bonding rule that allows square-packed bundles.

作者信息

Owen C H, DeRosier D J, Condeelis J

机构信息

Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110.

出版信息

J Struct Biol. 1992 Nov-Dec;109(3):248-54. doi: 10.1016/1047-8477(92)90037-b.

DOI:10.1016/1047-8477(92)90037-b
PMID:1296758
Abstract

The elongation factor 1a (EF-1a) of Dictyostelium discoideum is an actin crosslinking protein that gives rise to a unique kind of actin bundle. Purified actin and EF-1a were allowed to form bundles and then were characterized by electron microscopy, computed diffraction analysis, and modeling. In these bundles crosslinked actin filaments are rotated by 90 degrees relative to each other, whereas other known crosslinking proteins require filaments to be unrotated. Bundles of actin EF-1a would tend to exclude other actin bundling proteins. EF-1a can thus regulate the state of the actin cytoskeleton as well as regulate protein synthesis.

摘要

盘基网柄菌的延伸因子1a(EF-1a)是一种肌动蛋白交联蛋白,可形成一种独特的肌动蛋白束。将纯化的肌动蛋白和EF-1a制成束,然后通过电子显微镜、计算衍射分析和建模进行表征。在这些束中,交联的肌动蛋白丝彼此相对旋转90度,而其他已知的交联蛋白则要求丝不旋转。肌动蛋白EF-1a束倾向于排斥其他肌动蛋白束蛋白。因此,EF-1a可以调节肌动蛋白细胞骨架的状态以及调节蛋白质合成。

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Actin crosslinking protein EF-1a of Dictyostelium discoideum has a unique bonding rule that allows square-packed bundles.盘基网柄菌的肌动蛋白交联蛋白EF-1a具有独特的结合规则,可形成方形排列的束状结构。
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