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Nucleic Acids Research, 1994, Vol. 22, No. 13 2490-2497
© 1994

MOLECULAR BIOLOGY

Activation of RuvC Holliday junction resolvase in vitro

Rajvee Shah, Richard J. Bennett and Stephen C. West*

Imperial Cancer Research Fund, Clare Hall Laboratories South Mimms, Herts EN6 3LD, UK

*To whom corrspondence should be addressed

Received April 19, 1994. Revised June 3, 1994. Accepted June 3, 1994.

The Escherichia coli RuvC protein is an endonuclease that resolves Holliday junctions. In vitro, the protein shows efficient structure-specific binding of Holliday junctions, yet the rate of junction resolution is remarkably low. We have mapped the sites of cleavage on a synthetic junction through which a crossover canbranch migrate through 26 bp and find that ≥ 90% of the junctions were cleaved at one site. This observation of sequence-specific cleavage suggests that inefficient resolution may be due to DNA binding events which occur away from the cleavage site and are therefore non-productive. Holliday junction resolution by RuvC protein can be stimulated by a number of factors including: (i) the presence of Mn2+ (rather than Mg2+) as the divalent metal cofactor, (ii) alkaline pH ( ≤ 10), and (iii) elevated temperature. These observations may indicate that other proteins are required for efficient RuvC-mediated resolution.


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