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

被引:222
作者
Okuwaki, M
Matsumoto, K
Tsujimoto, M
Nagata, K
机构
[1] Univ Tsukuba, Inst Basic Med Sci, Dept Infect Biol, Tsukuba, Ibaraki 3058575, Japan
[2] RIKEN, Inst Phys & Chem Res, Lab Cellular Biochem, Wako, Saitama 3510198, Japan
关键词
acidic chaperone; chromatin; decondensation; nucleolus; nucleosome assembly;
D O I
10.1016/S0014-5793(01)02939-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:272 / 276
页数:5
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