The BRCT Domain Is a Phospho-Protein Binding Domain

Author:

Yu Xiaochun123,Chini Claudia Christiano Silva123,He Miao123,Mer Georges123,Chen Junjie123

Affiliation:

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.

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 G 2 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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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