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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| http://dx.doi.org/10.1093/nar/gkm530 | DOI Listing |
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Mammalian SNM1 is required for genome stability.
Mol Genet Metab
May 2008
Department of Molecular and Medical Genetics, Oregon Health & Sciences University, 3181 Sam Jackson Park Road, Portland, OR 97239, USA.
The protein encoded by SNM1 in Saccharomyces cerevisiae has been shown to act specifically in DNA interstrand crosslinks (ICL) repair. There are five mammalian homologs of SNM1, including Artemis, which is involved in V(D)J recombination. Cells from mice constructed with a disruption in the Snm1 gene are sensitive to the DNA interstrand crosslinker, mitomycin (MMC), as indicated by increased radial formation following exposure.
View Article and Find Full Text PDFThe hSNM1 protein is a DNA 5'-exonuclease.
Nucleic Acids Res
November 2007
Oregon Health & Science University, Department of Molecular and Medical Genetics, 3181 SW Sam Jackson Park Road, Mail Code L103, Portland, OR 97239-3098, USA.
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.
View Article and Find Full Text PDFTranslation of hSNM1 is mediated by an internal ribosome entry site that upregulates expression during mitosis.
DNA Repair (Amst)
May 2002
The Department of Molecular Genetics, M.D. Anderson Cancer Center, The University of Texas, Houston, TX 77030, USA.
SNM1 is involved in the repair of DNA interstrand cross-links (ICLs) in Saccharomyces cerevisiae and possibly in human cells, although relatively little is known about its biochemical function. The hSNM1 contains a long 5' untranslated region (5'UTR) predicted to fold into a complex secondary structure, and which contains numerous short open reading frames (ORFs). We show here using bicistronic constructs that human SNM1 mRNA contains an internal ribosome entry site (IRES) that generally suppresses translation, except during mitosis where translation is upregulated.
View Article and Find Full Text PDFhSnm1 colocalizes and physically associates with 53BP1 before and after DNA damage.
Mol Cell Biol
December 2002
Department of Molecular Genetics, M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
snm1 mutants of Saccharomyces cerevisiae have been shown to be specifically sensitive to DNA interstrand crosslinking agents but not sensitive to monofunctional alkylating agents, UV, or ionizing radiation. Five homologs of SNM1 have been identified in the mammalian genome and are termed SNM1, SNM1B, Artemis, ELAC2, and CPSF73. To explore the functional role of human Snm1 in response to DNA damage, we characterized the cellular distribution and dynamics of human Snm1 before and after exposure to DNA-damaging agents.
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