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The XPF\u22c5ERCC1 heterodimer changes the electrophoretic mobility of the DNA\u2013protein complex formed with the other five repair factors, but it does not confer additional specificity. By using proteins with peptide tags or antibodies to the repair factors in electrophoretic mobility shift assays, it was found that XPA, replication protein A, transcription factor IIH, XPG, and XPF\u22c5excision repair cross-complementing 1 but not XPC\u22c5HHR23B were present in the penultimate and ultimate dual incision complexes. Thus, it appears that XPC\u22c5HHR23B is a molecular matchmaker that participates in the assembly of the excision nuclease but is not present in the ultimate dual incision complex. The excision nuclease makes an assymmetric DNase I footprint of \u224830 bp around the damage and increases the DNase I sensitivity of the DNA on both sides of the footprint.<\/jats:p>","DOI":"10.1073\/pnas.95.12.6669","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:32:33Z","timestamp":1027679553000},"page":"6669-6674","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":152,"title":["Assembly, subunit composition, and footprint of human DNA repair excision nuclease"],"prefix":"10.1073","volume":"95","author":[{"given":"Mitsuo","family":"Wakasugi","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aziz","family":"Sancar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Biophysics, University of 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