XPC interacts with both HHR23B and HHR23A in vivo.
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.
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Department of Molecular Genetics, University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.
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Peterson
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Legerski
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002478:Cells, Cultured; D017124:Conserved Sequence; D017931:DNA Primers; D004260:DNA Repair; D045643:DNA Repair Enzymes; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004330:Drosophila; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D016133:Polymerase Chain Reaction; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D017386:Sequence Homology, Amino Acid; D014162:Transfection; D020798:Two-Hybrid System Techniques; D014983:Xeroderma Pigmentosum
D017931:DNA Primers; D004268:DNA-Binding Proteins; C513287:RAD23B protein, human; D011994:Recombinant Proteins; C501002:Xpc protein, mouse; C086985:RAD23A protein, human; C086984:XPC protein, human; D045643:DNA Repair Enzymes