Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-15102
Mol Cell Biol 1998 May 01;185:2748-57. doi: 10.1128/MCB.18.5.2748.
Show Gene links Show Anatomy links

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 .


???displayArticle.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.

???displayArticle.pubmedLink??? 9566894
???displayArticle.pmcLink??? PMC110654
???displayArticle.link??? Mol Cell Biol
???displayArticle.grants??? [+]

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