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EMBO Rep. 2001 Oct;2(10):933-8. Epub 2001 Sep 24.

Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.

Author information

1
Department of Biochemistry, Robert Wood Johnson Medical School-UMDNJ, 675 Hoes Lane, Piscataway, NJ 08854, USA.

Abstract

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 multi-ubiquitin (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.

PMID:
11571271
PMCID:
PMC1084081
DOI:
10.1093/embo-reports/kve203
[Indexed for MEDLINE]
Free PMC Article

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