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PMID: 2675966 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Discrimination between DNA sequences by the EcoRV restriction endonuclease.

Biochemistry ·Vol. 28 ·No. 15 ·1989-07-25 ·Pages 6198-207

Taylor JD, Halford SE

Abstract

The EcoRV restriction endonuclease cleaves not only its recognition sequence on DNA, GATATC, but also, at vastly reduced rates, a number of alternative DNA sequences. The plasmid pAT153 contains 12 alternative sites, each of which differs from the recognition sequence by one base pair. The EcoRV nuclease showed a marked preference for one particular site from among these alternatives. This noncognate site was located at the sequence GTTATC, and the mechanism of action of EcoRV at this site was analyzed. The mechanism differed from that at the cognate site in three respects. First, the affinity of the enzyme for the noncognate site was lower than that for the cognate site, but, by itself, this cannot account for the specificity of EcoRV as measured from the values of kcat/Km. Second, the enzyme had a lower affinity for Mg2+ when it was bound to the noncognate site than when it was bound to its cognate site: this appears to be a key factor in limiting the rates of DNA cleavage at alternative sites. Third, the reaction pathway at the noncognate site differed from that at the cognate site. At the former, the EcoRV enzyme cleaved first one strand of the DNA and then the other while at the latter, both strands were cut in one concerted reaction. The difference in reaction pathway allows DNA ligase to proofread the activity of EcoRV by selective repair of single-strand breaks at noncognate sites, as opposed to double-strand breaks at the cognate site. The addition of DNA ligase to reactions with EcoRV made no difference to product formation at the cognate site, but products from reactions at noncognate sites were no longer detected.

MeSH Terms
Base Sequence DNA DNA Ligases/metabolism DNA Repair Deoxyribonucleases, Type II Site-Specific/metabolism Escherichia coli/enzymology Kinetics Plasmids Protein Binding Substrate Specificity
Chemicals
DNA Deoxyribonucleases, Type II Site-Specific GATATC-specific type II deoxyribonucleases DNA Ligases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Taylor J D
Department of Biochemistry, School of Medical Sciences, University of Bristol, U.K.
Halford S E
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1989-07-25
Pages
6198-207
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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