The BRCT domain is a phospho-protein binding domain - PubMed (original) (raw)
. 2003 Oct 24;302(5645):639-42.
doi: 10.1126/science.1088753.
Affiliations
- PMID: 14576433
- DOI: 10.1126/science.1088753
The BRCT domain is a phospho-protein binding domain
Xiaochun Yu et al. Science. 2003.
Abstract
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.
Comment in
- Cell signaling. The BRCT domain: signaling with friends?
Caldecott KW. Caldecott KW. Science. 2003 Oct 24;302(5645):579-80. doi: 10.1126/science.1091463. Science. 2003. PMID: 14576410 No abstract available.
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