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组蛋白H1对海胆鞭毛微管的稳定作用。

Stabilization of sea urchin flagellar microtubules by histone H1.

作者信息

Multigner L, Gagnon J, Van Dorsselaer A, Job D

机构信息

Département de Biologie Moléculaire et Structurale, Unité INSERM 244, Grenoble, France.

出版信息

Nature. 1992 Nov 5;360(6399):33-9. doi: 10.1038/360033a0.

DOI:10.1038/360033a0
PMID:1436071
Abstract

Complex microtubule assemblies are essential components of eukaryotic cilia and flagella. They are extremely stable and are not affected by agents that normally induce polymer disassembly. The molecular basis of this microtubular stability is unknown, and it is not related to any feature of the constitutive tubulin. In sea urchin sperm flagella, axonemal microtubules are found to be stabilized by a protein identical to histone H1, a result that defines a new role for this histone and provides evidence for a concerted evolution of chromatin and microtubular structures.

摘要

复杂的微管组件是真核生物纤毛和鞭毛的重要组成部分。它们极其稳定,不受通常诱导聚合物解聚的试剂影响。这种微管稳定性的分子基础尚不清楚,且与组成型微管蛋白的任何特征无关。在海胆精子鞭毛中,发现轴丝微管由一种与组蛋白H1相同的蛋白质稳定,这一结果定义了这种组蛋白的新作用,并为染色质和微管结构的协同进化提供了证据。

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