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Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7.

http://www.ncbi.nlm.nih.gov/pubmed/9566894

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 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Cell Cycle Proteins | DNA Replication | DNA, Complementary | DNA-Binding Proteins | Humans | Male | Minichromosome Maintenance Complex Component 7 | Molecular Sequence Data | Nuclear Proteins | Ovum | Peptide Fragments | Phosphoproteins | Protein Binding | Proteins | Recombinant Proteins | Retinoblastoma Protein | Retinoblastoma-Like Protein p107 | Retinoblastoma-Like Protein p130 | Spermatozoa | Xenopus | Xenopus Proteins

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