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Originally published In Press as doi:10.1074/jbc.M003420200 on June 6, 2000

J. Biol. Chem., Vol. 275, Issue 33, 25540-25546, August 18, 2000
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A Conserved Nuclease Domain in the Archaeal Holliday Junction Resolving Enzyme Hjc*

Mamuka Kvaratskhelia, Benjamin N. Wardleworth, David G. Norman, and Malcolm F. WhiteDagger

From the Department of Biochemistry, University of Dundee, Dundee DD1 5EH

Holliday junction resolving enzymes are ubiquitous proteins that function in the pathway of homologous recombination, catalyzing the rearrangement and repair of DNA. They are metal ion-dependent endonucleases with strong structural specificity for branched DNA species. Whereas the eukaryotic nuclear enzyme remains unknown, an archaeal Holliday junction resolving enzyme, Hjc, has recently been identified. We demonstrate that Hjc manipulates the global structure of the Holliday junction into a 2-fold symmetric X shape, with local disruption of base pairing around the point of cleavage that occurs in a region of duplex DNA 3' to the point of strand exchange. Primary and secondary structural analysis reveals the presence of a conserved catalytic metal ion binding domain in Hjc that has been identified previously in several restriction enzymes. The roles of catalytic residues conserved within this domain have been confirmed by site-directed mutagenesis. This is the first example of this domain in an archaeal enzyme of known function as well as the first in a Holliday junction resolving enzyme.

* This work was funded by the Biotechnology and Biological Sciences Research Council.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger A Royal Society University Research Fellow. To whom correspondence should be addressed: Center for Biomolecular Sciences, St. Andrews University, North Haugh, St. Andrews KY 16 9ST, United Kingdom. Tel.: 01334-463432; Fax: 01334-462595; E-mail: mfw2@st- andrews.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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