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Vol. 10, Issue 12, 4043-4057, December 1999
The Salk Institute for Biological Studies, Molecular Biology and
Virology Laboratory, La Jolla, California 92037
The minichromosome maintenance (MCM) proteins MCM2-MCM7 are
conserved eukaryotic replication factors that assemble in a
heterohexameric complex. In fission yeast, these proteins are nuclear
throughout the cell cycle. In studying the mechanism that regulates
assembly of the MCM complex, we analyzed the cis and
trans elements required for nuclear localization of a
single subunit, Mcm2p. Mutation of any single mcm gene
leads to redistribution of wild-type MCM subunits to the cytoplasm, and
this redistribution depends on an active nuclear export system. We
identified the nuclear localization signal sequences of Mcm2p and
showed that these are required for nuclear targeting of other MCM
subunits. In turn, Mcm2p must associate with other MCM proteins for its
proper localization; nuclear localization of MCM proteins thus requires
assembly of MCM proteins in a complex. We suggest that coupling complex
assembly to nuclear targeting and retention ensures that only intact
heterohexameric MCM complexes remain nuclear.
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