Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA.
The structure of the Rad4/Rad23 protein, shown in a recent issue of Nature (Min and Pavletich, 2007), reveals how structurally diverse lesions are recognized in eukaryotic nucleotide excision repair: by probing for accessible nondamaged DNA opposite the lesion.
Schärer
Orlando D
OD
Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11974-3400, USA. orlando@pharm.stonybrook.edu
D004249:DNA Damage; D004260:DNA Repair; D004271:DNA, Fungal / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D051758:Transcription Factor TFIIH / Q000378:metabolism
D004271:DNA, Fungal; D004268:DNA-Binding Proteins; C490846:RAD23 protein, S cerevisiae; C493797:Rad4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D051758:Transcription Factor TFIIH