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Vol. 13, Issue 6, 2016-2030, June 2002
and
*Department of Infection Biology, Institute of Basic Medical
Sciences, University of Tsukuba, 1-1-1 Tennohdai, Tsukuba 305-8575, Japan; and Nucleophosmin/B23 is a nucleolar phosphoprotein. It has been shown
that B23 binds to nucleic acids, digests RNA, and is localized in
nucleolar granular components from which preribosomal particles are
transported to cytoplasm. The intracellular localization of B23 is
significantly changed during the cell cycle. Here, we have examined the
cellular localization of B23 proteins and the effect of mitotic
phosphorylation of B23.1 on its RNA binding activity. Two splicing
variants of B23 proteins, termed B23.1 and B23.2, were complexed both
in vivo and in vitro. The RNA binding activity of B23.1 was impaired by
hetero-oligomer formation with B23.2. Both subtypes of B23 proteins
were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding
activity of B23.1 was repressed through cyclin B/cdc2-mediated
phosphorylation at specific sites in B23. Thus, the RNA binding
activity of B23.1 is stringently modulated by its phosphorylation and
subtype association. Interphase B23.1 was mainly localized in nucleoli,
whereas B23.2 and mitotic B23.1, those of which were incapable of
binding to RNA, were dispersed throughout the nucleoplasm and
cytoplasm, respectively. These results suggest that nucleolar
localization of B23.1 is mediated by its ability to associate with RNA.
Laboratory of Cellular Biochemistry, RIKEN
(The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako
351-0198, Japan
Corresponding author. E-mail address:
knagata{at}md.tsukuba.ac.jp.
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