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XB-ART-15102
Mol Cell Biol May 1, 1998; 18 (5): 2748-57.
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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 .


Abstract
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.

PubMed ID: 9566894
PMC ID: PMC110654
Article link: Mol Cell Biol
Grant support: [+]

Species referenced: Xenopus
Genes referenced: mcm7 nolc1 rb1 rbl1

References [+] :
Bergemann, Sequence of cDNA comprising the human pur gene and sequence-specific single-stranded-DNA-binding properties of the encoded protein. 1992, Pubmed