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.
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
Science
Date: Oct. 24, 2003
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