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Nucleic Acids Research Advance Access first published online on September 5, 2007
This version published online on September 24, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm530
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

The hSNM1 protein is a DNA 5'-exonuclease

James Hejna, Sahaayaruban Philip, Jesse Ott, Craig Faulkner and Robb Moses*

Oregon Health & Science University, Department of Molecular and Medical Genetics, 3181 SW Sam Jackson Park Road, Mail Code L103, Portland, OR 97239-3098

*To whom correspondence should be addressed. Tel: +503 494 6881; Fax: +503 494 6886; Email: mosesr{at}ohsu.edu

Received April 30, 2007. Revised June 20, 2007. Accepted June 26, 2007.

The human SNM1 protein is a member of a highly conserved group of proteins catalyzing the hydrolysis of nucleic acid substrates. Although overproduction is unstable in mammalian cells, we have overproduced a recombinant hSNM1 protein in an insect cell system. The protein is a single-strand 5'-exonuclease, like its yeast homolog. The enzyme utilizes either DNA or RNA substrates, requires a 5'-phosphate moiety, shows very little activity on double-strand substrates, and functions at a size consistent with a monomer. The exonuclease activity requires the conserved ß-lactamase domain; site-directed mutagenesis of a conserved aspartate inactivates the exonuclease.


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