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J. Biol. Chem., Vol. 276, Issue 31, 29067-29071, August 3, 2001
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,
From the Department of Pathology, Brigham and Women's Hospital,
Harvard Medical School, Boston, Massachusetts 02115
All the human homologs of the six subunits of
Saccharomyces cerevisiae origin recognition complex have
been reported so far. However, not much has been reported on the nature
and the characteristics of the human origin recognition complex. In an
attempt to purify recombinant human ORC from insect cells infected with
baculoviruses expressing HsORC subunits, we found that human ORC2, -3, -4, and -5 form a core complex. HsORC1 and HsORC6 subunits did not
enter into this core complex, suggesting that the interaction of these two subunits with the core ORC2-5 complex is extremely labile. We
found that the C-terminal region of ORC2 interacts directly with the
N-terminal region of ORC3. The C-terminal region of ORC3 was, however,
necessary to bring ORC4 and ORC5 into the core complex. A fragment
containing the N-terminal 200 residues of ORC3 (ORC3N) competitively
inhibited the ORC2-ORC3 interaction. Overexpression of this fragment in
U2OS cells blocked the cells in G1, providing the first
evidence that a mammalian ORC subunit is important for the
G1-S transition in mammalian cells.
Supported by United States Army Postdoctoral Fellowship
DAMD17-00-1-0166.
§
Supported by the American Cancer Society Postdoctoral
Fellowship PF-99-328-01-CCG.
¶
To whom correspondence should be addressed: Dept. of
Pathology, Brigham and Women's Hospital, Harvard Medical School, 75 Francis St., Boston MA 02115. Tel.: 617-278-0468; Fax: 617-732-7449;
E-mail: adutta@rics.bwh.harvard.edu.
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