Abstract:
:The precise manner in which physical changes to the breast cancer susceptibility protein (BRCA1) affect its role in DNA repair events remain unclear. Indeed, cancer cells harboring mutations in BRCA1 suffer from genomic instability and increased DNA lesions. Here, we used a combination of molecular imaging and biochemical tools to study the properties of the BRCA1 in human cancer cells. Our results reveal new information for the manner in which full-length BRCA1 engages its binding partner, the BRCA1-associated Ring Domain protein (BARD1) under oxidative stress conditions. We also show how physical differences between wild type and mutated BRCA15382insC impact the cell's response to oxidative damage. Overall, we demonstrate how clinically relevant changes to BRCA1 affect its structure-function relationship in hereditary breast cancer.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Gilmore BL,Liang Y,Winton CE,Patel K,Karageorge V,Varano AC,Dearnaley W,Sheng Z,Kelly DFdoi
10.1038/srep43435subject
Has Abstractpub_date
2017-03-06 00:00:00pages
43435issn
2045-2322pii
srep43435journal_volume
7pub_type
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