Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA

Orlando D Schärer

doi:10.1016/j.molcel.2007.10.006

Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA

Mol Cell. 2007 Oct 26;28(2):184-6. doi: 10.1016/j.molcel.2007.10.006.

Author

Orlando D Schärer¹

Affiliation

¹ Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11974-3400, USA. orlando@pharm.stonybrook.edu

PMID: 17964258
DOI: 10.1016/j.molcel.2007.10.006

Abstract

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.

MeSH terms

DNA Damage*
DNA Repair*
DNA, Fungal / chemistry
DNA, Fungal / metabolism*
DNA-Binding Proteins / chemistry
DNA-Binding Proteins / metabolism*
Models, Molecular
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Saccharomyces cerevisiae / enzymology
Saccharomyces cerevisiae / genetics
Saccharomyces cerevisiae / metabolism*
Saccharomyces cerevisiae Proteins / chemistry
Saccharomyces cerevisiae Proteins / metabolism*
Transcription Factor TFIIH / metabolism

Substances

DNA, Fungal
DNA-Binding Proteins
RAD23 protein, S cerevisiae
Rad4 protein, S cerevisiae
Saccharomyces cerevisiae Proteins
Transcription Factor TFIIH