Covalent trapping of protein-DNA complexes.
High-resolution structural studies of protein-DNA complexes have proven to be an invaluable means of understanding the diverse functions of proteins that manage the genome. Most of the structures determined to date represent proteins bound noncovalently to various DNA sequences or structures. Although noncovalent complexation is often adequate to study the structures of proteins that have robust, specific interactions with DNA, it is poorly suited to the study of transient intermediates in enzyme-catalyzed DNA processing reactions or of complexes that exist in multiple equilibrating forms. In recent years, strategies developed for the covalent trapping of protein-DNA complexes have begun to show promise as a window into an otherwise inaccessible world of structure.
Verdine
Gregory L
GL
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. verdine@chemistry.harvard.edu
Norman
Derek P G
DP
D000818:Animals; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000378:metabolism; D004264:DNA Topoisomerases, Type I / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D004220:Disulfides / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D009699:N-Glycosyl Hydrolases / Q000378:metabolism; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation
D003432:Cross-Linking Reagents; D004268:DNA-Binding Proteins; D004220:Disulfides; D004247:DNA; D004248:DNA (Cytosine-5-)-Methyltransferases; D009699:N-Glycosyl Hydrolases; D004264:DNA Topoisomerases, Type I