XPC interacts with both HHR23B and HHR23A in vivo

Lei Li, Xiaoyan Lu, Carolyn Peterson, Randy Legerski

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

XP group C protein (XPC) and a human homologue of RAD23, HHR23B, have previously been shown to copurify in a tightly associated complex. Here, we show that XPC interacts in vivo, by means of the yeast two-hybrid system, with both HHR23B and a second homologue of RAD23, HHR23A. Domain mapping studies have revealed that both RAD23 homologues interact with XPC at the same highly conserved region in the C-terminal half of the protein. XPC mutants deleted within this domain and that are highly deficient in binding both RAD23 homologues are also highly defective in complementing XPC cells in vivo. Domain mapping studies have also identified a region in the N-terminal half of HHR23B that contains the XPC interactive site. This domain is highly conserved among HHR23B, HHR23A, and RAD23.

Original languageEnglish (US)
Pages (from-to)197-203
Number of pages7
JournalMutation Research - DNA Repair
Volume383
Issue number3
DOIs
StatePublished - May 1 1997

Keywords

  • Domain mapping
  • Nucleotide excision repair
  • Xeroderma pigmentosum
  • Xeroderma pigmentosum group C protein (XPC)

ASJC Scopus subject areas

  • Molecular Biology
  • Toxicology
  • Genetics

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