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Nucleic Acids Research, 1978, Vol. 5, No. 8 2991-2998
© 1978

Articles

Substrate dependence of the mechanism of EcoRI endonuclease

Robert A. Rubin and Paul Modrich*

Department of Biochemistry, Duke University Medical Center Durham, NC 27710, USA

Received May 25, 1978.

The mechanism of EcoRI endonuclease is substrate dependent. At 37°, dissociation of the enzyme-Form II DNA intermediates of ColE1 DNA and bacteriophage G4 RFI DNA is negligible. Therefore, both DNA strands with in the EcoRI sequence are cleaved during a single binding event. However, double strand cleavage of SV40 DNA occurs without dissociation of the enzyme in only 75% of the catalytic events. This mechanistic difference presumably reflects sequence differences about the EcoRI sites of these DNA's.

*To whom correspondence should be sent.


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D. J. Wright, W. E. Jack, and P. Modrich
The Kinetic Mechanism of EcoRI Endonuclease
J. Biol. Chem., November 5, 1999; 274(45): 31896 - 31902.
[Abstract] [Full Text] [PDF]


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