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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Okuwaki M,Matsumoto K,Tsujimoto M,Nagata K

doi

10.1016/s0014-5793(01)02939-8

keywords:

subject

Has Abstract

pub_date

2001-10-12 00:00:00

pages

272-6

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02939-8

journal_volume

506

pub_type

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