The hSNM1 protein is a DNA 5′-exonuclease

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

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

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 β-lactamase domain; site-directed mutagenesis of a conserved aspartate inactivates the exonuclease.

Original languageEnglish (US)
Pages (from-to)6115-6123
Number of pages9
JournalNucleic Acids Research
Volume35
Issue number18
DOIs
StatePublished - Sep 2007

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Exodeoxyribonucleases
Phosphodiesterase I
Exonucleases
Site-Directed Mutagenesis
Recombinant Proteins
Aspartic Acid
Nucleic Acids
Insects
Proteins
Hydrolysis
Yeasts
Phosphates
RNA
DNA
Enzymes

ASJC Scopus subject areas

  • Genetics

Cite this

Hejna, J., Philip, S., Ott, J., Faulkner, C., & Moses, R. (2007). The hSNM1 protein is a DNA 5′-exonuclease. Nucleic Acids Research, 35(18), 6115-6123. https://doi.org/10.1093/nar/gkm530

The hSNM1 protein is a DNA 5′-exonuclease. / Hejna, James; Philip, Sahaayaruban; Ott, Jesse; Faulkner, Craig; Moses, Robb.

In: Nucleic Acids Research, Vol. 35, No. 18, 09.2007, p. 6115-6123.

Research output: Contribution to journalArticle

Hejna, J, Philip, S, Ott, J, Faulkner, C & Moses, R 2007, 'The hSNM1 protein is a DNA 5′-exonuclease', Nucleic Acids Research, vol. 35, no. 18, pp. 6115-6123. https://doi.org/10.1093/nar/gkm530
Hejna, James ; Philip, Sahaayaruban ; Ott, Jesse ; Faulkner, Craig ; Moses, Robb. / The hSNM1 protein is a DNA 5′-exonuclease. In: Nucleic Acids Research. 2007 ; Vol. 35, No. 18. pp. 6115-6123.
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