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Nucleic Acids Research, 2001, Vol. 29, No. 18 3757-3774
© 2001 Oxford University Press


Survey and Summary

Homing endonucleases: structural and functional insight into the catalysts of intron/intein mobility

Brett S. Chevalier and Barry L. Stoddard*

Division of Basic Sciences, Fred Hutchinson Cancer Research Center and Graduate Program in Molecular and Cell Biology, University of Washington, 1100 Fairview Avenue North A3-023, Seattle, WA 98109, USA

Homing endonucleases confer mobility to their host intervening sequence, either an intron or intein, by catalyzing a highly specific double-strand break in a cognate allele lacking the intervening sequence. These proteins are characterized by their ability to bind long DNA target sites (14–40 bp) and their tolerance of minor sequence changes in these sites. A wealth of biochemical and structural data has been generated for these enzymes over the past few years. Herein we review our current understanding of homing endonucleases, including their diversity and evolution, DNA-binding and catalytic mechanisms, and attempts to engineer them to bind novel DNA substrates.

* To whom correspondence should be addressed. Tel: +1 206 667 4031; Fax: +1 206 667 6877; Email: bstoddar{at}fred.fhcrc.org


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