title: Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition.
abstract: Nucleotide excision repair is an important and highly conserved DNA repair mechanism with an exceptionally large range of chemically and structurally unrelated targets. Lesion verification is believed to be achieved by the helicases UvrB and XPD in the prokaryotic and eukaryotic processes, respectively. Using single molecule atomic force microscopy analyses, we demonstrate that UvrB and XPD are able to load onto DNA and pursue lesion verification in the absence of the initial lesion detection proteins. Interestingly, our studies show different lesion recognition strategies for the two functionally homologous helicases, as apparent from their distinct DNA strand preferences, which can be rationalized from the different structural features and interactions with other nucleotide excision repair protein factors of the two enzymes.
authors.affiliation: From the Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Wirth
authors.affiliation: From the Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany.
authors.forename: Jonas
authors.initials: J
authors.lastname: Gross
authors.affiliation: From the Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany.
authors.forename: Heide M
authors.initials: HM
authors.lastname: Roth
authors.affiliation: From the Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany.
authors.forename: Claudia N
authors.initials: CN
authors.lastname: Buechner
authors.affiliation: From the Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany.
authors.forename: Caroline
authors.initials: C
authors.lastname: Kisker
authors.affiliation: From the Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany ingrid.tessmer@virchow.uni-wuerzburg.de.
authors.forename: Ingrid
authors.initials: I
authors.lastname: Tessmer
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004265:DNA Helicases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004260:DNA Repair; D004269:DNA, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004265:DNA Helicases
keywords: DNA helicase; DNA lesion recognition; DNA repair; UvrB; XPD; atomic force microscopy (AFM); nucleotide excision repair; protein-DNA interaction; single-molecule biophysics