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 RIS Download
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
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