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
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.
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