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J. Biol. Chem., Vol. 275, Issue 25, 18871-18878, June 23, 2000
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From the Graduate Program in Molecular Biology, Memorial
Sloan-Kettering Cancer Center, New York, New York 10021
Minichromosome maintenance (Mcm) proteins 2-7
are highly conserved in eukaryotes and play an essential role in DNA
replication. Here, we describe the reconstitution of the various
complexes of the Mcm proteins of Schizosaccharomyces pombe
using the baculovirus expression system. The simultaneous expression of
all six of the Mcm proteins, as well as different combinations of these
proteins, yielded several stable complexes that included the
heterohexamer of Mcm2/3/4/5/6/7, the Mcm2/4/6/7 heterotetramer, the
dimer of the Mcm4/6/7 heterotrimer, and the Mcm3/5 heterodimer. The
purification and characterization of the biochemical properties of
these complexes showed that only the dimeric complex of the Mcm4/6/7
heterotrimer possessed single stranded DNA-dependent
ATPase, ATP-dependent single stranded DNA binding, and 3'
to 5' DNA helicase activities. Consistent with these results, the
interaction of either Mcm2 or Mcm3/5 with the Mcm4/6/7 complex resulted
in the disassembly of the dimeric complex of Mcm4/6/7 and the loss of
DNA helicase activity. These results suggest that the Mcm4/6/7 complex
is a catalytic core of the Mcm complex and that Mcm2 and Mcm3/5 may be
involved in the regulation of the activity of this complex.
To whom correspondence should be addressed. Fax: 212-717-3627;
E-mail: j-hurwitz@ski.mskcc.org.
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B. K. Tye and S. Sawyer The Hexameric Eukaryotic MCM Helicase: Building Symmetry from Nonidentical Parts J. Biol. Chem., November 3, 2000; 275(45): 34833 - 34836. [Full Text] [PDF]
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