Journal
NUCLEIC ACIDS RESEARCH
Volume 35, Issue 18, Pages 6115-6123Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkm530
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Funding
- NHLBI NIH HHS [5P01HL048546, P01 HL048546] Funding Source: Medline
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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 beta-lactamase domain; site-directed mutagenesis of a conserved aspartate inactivates the exonuclease.
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