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FEBS Lett. 2001 Oct 12;506(3):272-6.

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

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1
Laboratory of Cellular Biochemistry, RIKEN (The Institute of Physical and Chemical Research), Wako, Japan.

Abstract

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.

PMID:
11602260
DOI:
10.1016/s0014-5793(01)02939-8
[Indexed for MEDLINE]
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