Type II restriction endonucleases.
Type II restriction endonucleases have emerged as important paradigms for the study of protein-nucleic acid interactions. This is due to their ability to catalyse phosphodiester bond cleavage with very large rate enhancements while also maintaining exquisite sequence selectivities. The principles and methods developed to analyze site-specific binding and catalysis for restriction endonucleases can be applied to other enzymes which also operate on nucleic acids. This paper reviews biochemical and structural approaches to characterization of these enzymes, with particular attention to the multiple crucial roles of divalent metal ions, the possibilities for use of alternative substrates in binding and catalytic experiments, the strategies for exploring the detailed chemistry of phosphoryl transfer, and the use of X-ray crystallography to provide descriptions of conformational pathways at specific, nonspecific, and noncognate DNA sites.
Perona
John J
JJ
Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106-9510, USA. perona@chem.ucsb.edu
D003461:Crystallography; D004247:DNA / Q000378:metabolism; D004262:DNA Restriction Enzymes / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D009838:Oligodeoxyribonucleotides / Q000378:metabolism; D010957:Plasmids; D011485:Protein Binding
D009838:Oligodeoxyribonucleotides; D004247:DNA; D004262:DNA Restriction Enzymes; D008274:Magnesium