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Papers In Press, published online ahead of print January 24, 2001
J. Biol. Chem, 10.1074/jbc.M011556200
Submitted on December 21, 2000
Revised on January 22, 2001
Accepted on January 23, 2001
Department of Genetics, Duke University Medical Center, Durham, NC 27710
Corresponding Author: J.Nevins{at}Duke.Edu
Summary: 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 (HAT) domain. Biochemical studies confirmed the interaction between MCM2 and HBO1 in vitro and in vivo. An amino-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.
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