[HTML][HTML] Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein
The breast and ovarian cancer-specific tumor suppressor RING finger protein BRCA1 has
been identified as an E3 ubiquitin (Ub) ligase through in vitro studies, which demonstrated
that its RING finger domain can autoubiquitylate and monoubiquitylate histone H2A when
supplied with Ub, E1, and UBC4 (E2). Here we report that the E3 ligase activity of the N-
terminal 110 amino acid residues of BRCA1, which encodes a stable domain containing the
RING finger, as well as that of the full-length BRCA1, was significantly enhanced by the …
been identified as an E3 ubiquitin (Ub) ligase through in vitro studies, which demonstrated
that its RING finger domain can autoubiquitylate and monoubiquitylate histone H2A when
supplied with Ub, E1, and UBC4 (E2). Here we report that the E3 ligase activity of the N-
terminal 110 amino acid residues of BRCA1, which encodes a stable domain containing the
RING finger, as well as that of the full-length BRCA1, was significantly enhanced by the …