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Science 302 (5645): 639-642

Copyright © 2003 by the American Association for the Advancement of Science

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*

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.

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}

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BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP..
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Genes & Dev. 20, 1721-1726
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Small carboxyl-terminal domain phosphatase 2 attenuates androgen-dependent transcription.
J. Thompson, T. Lepikhova, N. Teixido-Travesa, M. A. Whitehead, J. J. Palvimo, and O. A. Janne (2006)
EMBO J. 25, 2757-2767
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