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Cited by 538

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A DNA Helicase Activity Is Associated with an MCM4, -6, and -7 Protein Complex

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Ishimi, Yukio·1997·Journal of Biological Chemistry

Abstract

All six minichromosome maintenance (MCM) proteins have DNA-dependent ATPase motifs in the central domain which is conserved from yeast to mammals. Our group purified MCM protein complexes consisting of MCM2, -4 (Cdc21), -6 (Mis5), and -7 (CDC47) proteins from HeLa cells by using histone-Sepharose column chromatography (Ishimi, Y., Ichinose, S., Omori, A., Sato K., and Kimura, H. (1996) J. Biol. Chem. 271, 24115-24122). The present study revealed that both ATPase activity and DNA helicase activity that displaces oligonucleotides annealed to single-stranded circular DNA are associated with an MCM protein complex. Both ATPase and DNA helicase activities were co-purified with a 600-kDa protein complex that is consisted of equal amounts of MCM4, -6, and -7 proteins. An immunodepletion of the MCM protein complex from the purified fraction using anti-MCM4 antibody resulted in the severe reduction of the DNA helicase activity. Displacement of DNA fragments by the DNA helicase suggested that it migrated along single-stranded DNA in the 3' to 5' direction, and the DNA helicase activity was detected only in the presence of hydrolyzable ATP or dATP. These results suggest that this helicase may be involved in the initiation of DNA replication as a DNA unwinding enzyme.

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Metadata

Authors
Ishimi, Y.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-09
Volume
272
Issue
39
Pages
24508-24513
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2093703127
Cited by
538
References
1
FWCI
9.79
Type
journal article
Language
en
Open access
hybrid

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