Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 387, Issue 1, Pages 10-16Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.01.048
Keywords
restriction endonuclease; Eco29kI; DNA-protein interaction; protein dimerization; GIY-YIG family
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Funding
- European Commission 5th Framework Programme [QLK2-CT-2002-30575]
- Russian Foundation for Basic Research [04-04-48784-a, 06-04-49667-a]
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The GIY-YIG nuclease domain has been identified in homing endonucleases, DNA repair and recombination enzymes, and restriction endonucleases. The Type H restriction enzyme Eco29kI belongs to the GIY-YIG nuclease superfamily and, like most of other family members, including the homing endonuclease I-TevI, is a monomer. It recognizes the palindromic sequence 5'-CCGC/GG-3' (/ marks the cleavage position) and cuts it to generate 3'-staggered ends. The Eco29kI monomer, which contains a single active site, either has to nick sequentially individual DNA strands or has to form dimers or even higher-order oligomers upon DNA binding to make a double-strand break at its target site. Here, we provide experimental evidence that Eco29kI monomers dimerize on a single cognate DNA molecule forming the catalytically active complex. The mechanism described here for Eco29kI differs from that of Cfr42I isoschisomer, which also belongs to the GIY-YIG family but is functional as a tetramer. This novel mechanism may have implications for the function of homing endonucleases and other enzymes of the GIY-YIG family. (C) 2009 Elsevier Ltd. All rights reserved.
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