XB-ART-15102
Mol Cell Biol
1998 May 01;185:2748-57. doi: 10.1128/MCB.18.5.2748.
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Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7.
Sterner JM
,
Dew-Knight S
,
Musahl C
,
Kornbluth S
,
Horowitz JM
.
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A yeast two-hybrid screen was employed to identify human proteins that specifically bind the amino-terminal 400 amino acids of the retinoblastoma (Rb) protein. Two independent cDNAs resulting from this screen were found to encode the carboxy-terminal 137 amino acids of MCM7, a member of a family of proteins that comprise replication licensing factor. Full-length Rb and MCM7 form protein complexes in vitro, and the amino termini of two Rb-related proteins, p107 and p130, also bind MCM7. Protein complexes between Rb and MCM7 were also detected in anti-Rb immunoprecipitates prepared from human cells. The amino-termini of Rb and p130 strongly inhibited DNA replication in an MCM7-dependent fashion in a Xenopus in vitro DNA replication assay system. These data provide the first evidence that Rb and Rb-related proteins can directly regulate DNA replication and that components of licensing factor are targets of the products of tumor suppressor genes.
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CA53248 NCI NIH HHS
Species referenced: Xenopus
Genes referenced: mcm7 nolc1 rb1 rbl1
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