期刊
EMBO REPORTS
卷 2, 期 10, 页码 933-938出版社
OXFORD UNIV PRESS
DOI: 10.1093/embo-reports/kve203
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资金
- NCI NIH HHS [R01 CA083875, CA-83875] Funding Source: Medline
Rad23 is a DNA repair protein that promotes the assembly of the nucleotide excision repair complex. Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and inhibits the assembly of substrate-linked multiubiquitin (multi-Ub) chains in vitro and in vivo. Significantly, Rad23 can bind a proteolytic substrate that is conjugated to a few ubiquitin (Ub) moieties. We report here that two ubiquitin-associated (UBA) domains in Rad23 form non-covalent interactions with Ub. A mutant that lacked either UBA sequence was capable of blocking the assembly of substrate-linked multi-Ub chains, although a mutant that lacked both UBA domains was significantly impaired. These studies suggest that the interaction with Ub is required for Rad23 activity and that other UBA-containing proteins may have a similar function.
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