BRCA1 BRCT domains (human recombinant)

Description

The BRCA1 C-terminal (BRCT) domain is a modular unit of ~100 amino acids that folds independently and recognizes linear phosphoserine or phosphothreonine regions to mediate protein-protein and protein-DNA interactions. BRCT domains were initially recognized in the C-terminal region of the breast cancer protein BRCA1, as well as the p53 binding protein (53BP1; TP53BP1), and the yeast cell cycle checkpoint protein RAD9. BRCT domains often occur as tandem repeats at the C-terminal end of several proteins that are functionally diverse. Most BRCT domain-containing proteins participate in DNA-damage checkpoint control or DNA-repair pathways, or both. Thus, BRCT domain-containing proteins likely participate in the cellular response to DNA damage.Germ-line mutations of the tumor suppressor genes BRCA1 and BRCA2 pre-dispose women to familial breast and ovarian cancer and are associated with approximately 10% of the cases. The carboxy-terminal BRCT domain in BRCA1 is involved in DNA repair and transcriptional activation. The BRCT region of BRCA1 binds phosphorylated BACH1, a DEAH helicase, which is essential for mediating repair of DNA double-strand breaks by controlling G₂ to M phase transition during cell cycle progression. BRCA1 also contains an N-terminal protein-protein-interaction RING-finger domain, that partners with BRCA1-associated RING domain 1 (BARD1). The BRCA1/BARD1 heterodimer maintains genomic stability by regulating DNA damage repair and ubiquitination. This product contains the BRCT domains of BRCA1.

References

[1] ISAAC A. MANKE. BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting[J]. Science, 2003, 302 5645. DOI: 10.1126/science.1088877
[2] NICHOLAS T. WOODS, JR. Charting the Landscape of Tandem BRCT Domain–Mediated Protein Interactions[J]. Science Signaling, 2012, 5 242. DOI: 10.1126/scisignal.2002255
[3] P BORK. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.[J]. FASEB Journal, 1997, 11 1: 68-76.
[4] ISABELLE CALLEBAUT  Jean P M. From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair[J]. FEBS Letters, 1998, 400 1: 25-30. DOI: 10.1016/s0014-5793(96)01312-9
[5] PETER J O’DONOVAN  David M L. BRCA1 and BRCA2: breast/ovarian cancer susceptibility gene products and participants in DNA double-strand break repair.[J]. Carcinogenesis, 2010, 31 6: 961-967. DOI: 10.1093/carcin/bgq069
[6] RONIT I YARDEN  Moshe Z P. BRCA1 at the crossroad of multiple cellular pathways: approaches for therapeutic interventions.[J]. Molecular Cancer Therapeutics, 2006, 5 6: 1396-1404. DOI: 10.1158/1535-7163.mct-05-0471
[7] KELLY A METCALFE  Steven A N. Breast cancer prevention in women with a BRCA1 or BRCA2 mutation.[J]. Open medicine: a peer-reviewed, independent, open-access journal, 2007, 1 3: e184-90.
[8] NAROD S A. Modifiers of risk of hereditary breast and ovarian cancer[J]. Nature Reviews Cancer, 2002, 2 2: 113-123. DOI: 10.1038/nrc726
[9] ERIC N SHIOZAKI. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling.[J]. Molecular Cell, 2004, 14 3: 405-412. DOI: 10.1016/s1097-2765(04)00238-2
[10] SHARON B. CANTOR. BACH1, a Novel Helicase-like Protein, Interacts Directly with BRCA1 and Contributes to Its DNA Repair Function[J]. Cell, 2001, 105 1: 149-160. DOI: 10.1016/s0092-8674(01)00304-x
[11] XIAOCHUN YU. The BRCT Domain Is a Phospho-Protein Binding Domain[J]. Science, 2003, 302 5645. DOI: 10.1126/science.1088753
[12] HIROYUKI NISHIKAWA. BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity.[J]. Cancer research, 2009: 111-119. DOI: 10.1158/0008-5472.can-08-3355
[13] PETER S BRZOVIC. Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex.[J]. Proceedings of the National Academy of Sciences of the United States of America, 2003, 100 10: 5646-5651. DOI: 10.1073/pnas.0836054100