Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone.
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.
Okuwaki
M
M
Laboratory of Cellular Biochemistry, RIKEN (The Institute of Physical and Chemical Research), Wako, Japan.
Matsumoto
K
K
Tsujimoto
M
M
Nagata
K
K
D002466:Cell Nucleolus / Q000378:metabolism*; D006367:HeLa Cells; D006657:Histones / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D009687:Nuclear Proteins / Q000502:physiology*; D000090243:Nucleophosmin
D006657:Histones; D018832:Molecular Chaperones; C000716967:NPM1 protein, human; D009687:Nuclear Proteins; D000090243:Nucleophosmin