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

FEBS Letters

Matsumoto, Ken¹  Tsujimoto, Masafumi¹  Nagata, Kyosuke²  Okuwaki, Mitsuru¹ 

[1] Laboratory of Cellular Biochemistry, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako 351-0198, Japan;Department of Infection Biology, Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1 Tennohdai, Tsukuba 305-8575, Japan

关键词: Acidic chaperone;    Chromatin;    Decondensation;    Nucleolus;    Nucleosome assembly;   

DOI  :  10.1016/S0014-5793(01)02939-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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/B23 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.

【 授权许可】

Unknown