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The BRCT domain is a phospho-protein binding domain.

The carboxyl-terminal domain (BRCT) of the Breast Cancer Gene 1 (BRCA1) protein is an evolutionarily conserved module that exists in a large number of proteins from prokaryotes to eukaryotes. Although most BRCT domain-containing proteins participate in DNA-damage checkpoint or DNA-repair pathways, or both, the function of the BRCT domain is not fully understood. We show that the BRCA1 BRCT domain directly interacts with phosphorylated BRCA1-Associated Carboxyl-terminal Helicase (BACH1). This specific interaction between BRCA1 and phosphorylated BACH1 is cell cycle regulated and is required for DNA damage-induced checkpoint control during the transition from G2 to M phase of the cell cycle. Further, we show that two other BRCT domains interact with their respective physiological partners in a phosphorylation-dependent manner. Thirteen additional BRCT domains also preferentially bind phospho-peptides rather than nonphosphorylated control peptides. These data imply that the BRCT domain is a phospho-protein binding domain involved in cell cycle control.

Pubmed ID: 14576433


  • Yu X
  • Chini CC
  • He M
  • Mer G
  • Chen J


Science (New York, N.Y.)

Publication Data

October 24, 2003

Associated Grants

  • Agency: NCI NIH HHS, Id: CA89239
  • Agency: NCI NIH HHS, Id: CA92312

Mesh Terms

  • Amino Acid Motifs
  • BRCA1 Protein
  • Carrier Proteins
  • Cell Cycle
  • Cell Cycle Proteins
  • Cell Line
  • DNA Damage
  • DNA Repair
  • DNA-Binding Proteins
  • E2F Transcription Factors
  • G2 Phase
  • Humans
  • Mitosis
  • Mutation
  • Nuclear Proteins
  • Peptide Library
  • Phosphoprotein Phosphatases
  • Phosphoproteins
  • Phosphorylation
  • Phosphoserine
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA Helicases
  • RNA Polymerase II
  • RNA, Small Interfering
  • Recombinant Fusion Proteins
  • Transcription Factors
  • Transfection
  • Tumor Cells, Cultured