4.5 Article

Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone

期刊

FEBS LETTERS
卷 506, 期 3, 页码 272-276

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)02939-8

关键词

acidic chaperone; chromatin; decondensation; nucleolus; nucleosome assembly

向作者/读者索取更多资源

We previously identified and purified a nucleolar phosphoprotein, nucleophosmin/B23, as a stimulatory factor for replication from the adenovirus chromatin. We show here that nucleophosmin/B23 functions as a histone chaperone protein such as nucleoplasmin, TAF-I, and NAP-I. Nucleophosmin/1323 was shown to bind to histones, preferentially to histone H3, to mediate formation of nucleosome, and to decondense sperm chromatin. These activities of B23 were dependent on its acidic regions as other histone chaperones, suggesting that B23/nucleophosmin is a member of histone chaperone proteins. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据