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(Received for publication, March 28, 1996, and in revised form, May 28, 1996)
From the Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194, Japan and § Research Center
for Molecular Genetics, Hokkaido University, Kita 10 Nishi 8, Kita-ku,
Sapporo 060, Japan
Minichromosome maintenance (MCM) proteins play
essential roles in eukaryotic DNA replication, but their biochemical
properties remain to be determined. We detected in HeLa cell extracts
six proteins, CDC47, CDC46/MCM5, Cdc21, P1/MCM3, Mis5, and BM28/MCM2,
by their binding to a specific antibody and by partial sequencing. The
human homologs of the MCM2 (BM28), Mis5, Cdc21, and CDC47 proteins were
tightly bound to a histone-Sepharose column and purified to near
homogeneity, whereas the P1/MCM3 and CDC46/MCM5 proteins passed
through. Among the four core histones, the human BM28/MCM2, Mis5,
Cdc21, and CDC47 proteins had high affinity for histone H3.
Immunoprecipitation with anti-Cdc21 antibody revealed that these four
MCM proteins form complexes. These results are consistent with the
findings that MCM proteins bind with chromatin in vivo.
Volume 271, Number 39,
Issue of September 27, 1996
pp. 24115-24122
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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