[HTML][HTML] Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase
H Nishikawa, S Ooka, K Sato, K Arima… - Journal of Biological …, 2004 - ASBMB
The breast and ovarian cancer suppressor BRCA1 acquires significant ubiquitin ligase
activity when bound to BARD1 as a RING heterodimer. Although the activity may well be
important for the role of BRCA1 as a tumor suppressor, the biochemical consequence of the
activity is not yet known. Here we report that BRCA1-BARD1 catalyzes Lys-6-linked
polyubiquitin chain formation. K6R mutation of ubiquitin dramatically reduces the
polyubiquitin products mediated by BRCA1-BARD1 in vitro. BRCA1-BARD1 preferentially …
activity when bound to BARD1 as a RING heterodimer. Although the activity may well be
important for the role of BRCA1 as a tumor suppressor, the biochemical consequence of the
activity is not yet known. Here we report that BRCA1-BARD1 catalyzes Lys-6-linked
polyubiquitin chain formation. K6R mutation of ubiquitin dramatically reduces the
polyubiquitin products mediated by BRCA1-BARD1 in vitro. BRCA1-BARD1 preferentially …