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

L. Chen, U. Shinde, T. G. Ortolan, K. Madura

Research output: Contribution to journalArticlepeer-review

165 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)933-938
Number of pages6
JournalEMBO Reports
Volume2
Issue number10
DOIs
StatePublished - 2001

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

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