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J. Biol. Chem., Vol. 276, Issue 18, 15397-15408, May 4, 2001
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,
From the Department of Genetics, Howard Hughes Medical Institute,
Duke University Medical Center, Durham, North Carolina 27710
The minichromosome maintenance (MCM) proteins,
together with the origin recognition complex (ORC) proteins and Cdc6,
play an essential role in eukaryotic DNA replication through the
formation of a pre-replication complex at origins of replication. We
used a yeast two-hybrid screen to identify MCM2-interacting proteins. One of the proteins we identified is identical to the ORC1-interacting protein termed HBO1. HBO1 belongs to the MYST family, characterized by
a highly conserved C2HC zinc finger and a putative
histone acetyltransferase domain. Biochemical studies confirmed the
interaction between MCM2 and HBO1 in vitro and in
vivo. An N-terminal domain of MCM2 is necessary for binding to
HBO1, and a C2HC zinc finger of HBO1 is essential for
binding to MCM2. A reverse yeast two-hybrid selection was performed to
isolate an allele of MCM2 that is defective for interaction with HBO1;
this allele was then used to isolate a suppressor mutant of HBO1 that
restores the interaction with the mutant MCM2. This suppressor mutation
was located in the HBO1 zinc finger. Taken together, these findings
strongly suggest that the interaction between MCM2 and HBO1 is direct
and mediated by the C2HC zinc finger of HBO1. The
biochemical and genetic interactions of MYST family protein HBO1 with
two components of the replication apparatus, MCM2 and ORC1, suggest
that HBO1-associated HAT activity may play a direct role in the process
of DNA replication.
Supported by an American Cancer Society Fellowship
PF-99-111-01-CCG.
§
Supported by an American Cancer Society Fellowship PF-4465.
¶
Supported by the Viral Oncology Training Grant CA09111-25 from
the National Institutes of Health.
Investigator of the Howard Hughes Medical Institute. To whom
correspondence should be addressed: Tel.: 919-684-2746; Fax: 919-681-8973; E-mail: j.nevins@duke.edu.
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