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

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

Authors

  • Sterner JM
  • Dew-Knight S
  • Musahl C
  • Kornbluth S
  • Horowitz JM

Journal

Molecular and cellular biology

Publication Data

May 21, 1998

Associated Grants

  • Agency: NCI NIH HHS, Id: CA53248

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