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猪脑19K蛋白对肌动蛋白聚合的作用:一类新的肌动蛋白结合蛋白的功能特性

Action of a 19K protein from porcine brain on actin polymerization: a new functional class of actin-binding proteins.

作者信息

Nishida E, Maekawa S, Muneyuki E, Sakai H

出版信息

J Biochem. 1984 Feb;95(2):387-98. doi: 10.1093/oxfordjournals.jbchem.a134619.

Abstract

A 19K protein isolated from porcine brain not only inhibits actin polymerization but depolymerizes actin filaments quickly. The protein reacts stoichiometrically with actin in a 1:1 molar ratio. When actin is induced to polymerize with salts in the presence of the brain 19K protein, the lag phase is prolonged, and the extent of polymerization is decreased, but the half-polymerization time is not increased. This can be explained by assuming that the 19K protein severs growing actin filaments and thus causes an increase in the number of filament ends during the polymerization process, thereby accelerating the overall polymerization. Moreover, the low-shear viscosity of actin filaments is reduced much more than the high-shear viscosity by the 19K protein, suggesting that actin filaments become shorter in the presence of the 19K protein than in its absence. Actin filament depolymerization by the 19K protein is much faster than that by brain profilin or than spontaneous depolymerization. This indicates that the 19K protein depolymerizes actin filaments not only by sequestering actin monomers but also by directly attacking the filaments. The number of actin filaments, measured by assaying the nucleating ability, is increased by substoichiometric concentrations of the 19K protein, irrespective of whether the protein is added to actin monomers before polymerization or added to performed actin filaments. These results suggest that the brain 19K protein not only stabilizes actin monomers but also cuts actin filaments, thereby decreasing the extent of actin polymerization and also changing the filament length. The action on actin of the actin-depolymerizing protein from starfish oocytes resembles that of the brain 19K protein, although the molecular weight of the starfish protein is slightly smaller. The brain 19K protein and starfish protein should be classified into a new functional group of actin-binding proteins.

摘要

从猪脑中分离出的一种19K蛋白不仅能抑制肌动蛋白聚合,还能迅速使肌动蛋白丝解聚。该蛋白与肌动蛋白以1:1的摩尔比进行化学计量反应。当在脑19K蛋白存在的情况下,用盐诱导肌动蛋白聚合时,延迟期延长,聚合程度降低,但半聚合时间并未增加。这可以通过假设19K蛋白切断正在生长的肌动蛋白丝来解释,从而在聚合过程中导致丝端数量增加,进而加速整体聚合。此外,19K蛋白使肌动蛋白丝的低剪切粘度比高剪切粘度降低得更多,这表明在19K蛋白存在下,肌动蛋白丝比不存在时更短。19K蛋白引起的肌动蛋白丝解聚比脑肌动蛋白解聚蛋白或自发解聚要快得多。这表明19K蛋白使肌动蛋白丝解聚不仅是通过隔离肌动蛋白单体,还通过直接攻击肌动蛋白丝。通过测定成核能力来测量的肌动蛋白丝数量,在亚化学计量浓度的19K蛋白作用下会增加,无论该蛋白是在聚合前添加到肌动蛋白单体中,还是添加到已形成的肌动蛋白丝中。这些结果表明,脑19K蛋白不仅能稳定肌动蛋白单体,还能切断肌动蛋白丝,从而降低肌动蛋白聚合程度并改变丝的长度。海星卵母细胞中肌动蛋白解聚蛋白对肌动蛋白的作用与脑19K蛋白相似,尽管海星蛋白的分子量略小。脑19K蛋白和海星蛋白应被归类为肌动蛋白结合蛋白的一个新功能组。

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