Journal
EMBO REPORTS
Volume 2, Issue 10, Pages 933-938Publisher
OXFORD UNIV PRESS
DOI: 10.1093/embo-reports/kve203
Keywords
-
Categories
Funding
- NCI NIH HHS [R01 CA083875, CA-83875] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available