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Science 24 October 2003:
Vol. 302. no. 5645, pp. 639 - 642
DOI: 10.1126/science.1088753
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Reports

The BRCT Domain Is a Phospho-Protein Binding Domain

Xiaochun Yu,1 Claudia Christiano Silva Chini,1 Miao He,2 Georges Mer,3 Junjie Chen1*

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.

1 Department of Oncology, Mayo Clinic and Foundation, Rochester, MN 55905, USA.
2 Department of Medical Genetics, Mayo Clinic and Foundation, Rochester, MN 55905, USA.
3 Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, MN 55905, USA.

* To whom correspondence should be addressed. E-mail: chen.junjie{at}mayo.edu

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