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The hSNM1 protein is a DNA 5′-exonuclease

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′-exonuc...

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Detalles Bibliográficos
Autores principales: Hejna, James, Philip, Sahaayaruban, Ott, Jesse, Faulkner, Craig, Moses, Robb
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2094091/
https://www.ncbi.nlm.nih.gov/pubmed/17804464
http://dx.doi.org/10.1093/nar/gkm530
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author Hejna, James
Philip, Sahaayaruban
Ott, Jesse
Faulkner, Craig
Moses, Robb
author_facet Hejna, James
Philip, Sahaayaruban
Ott, Jesse
Faulkner, Craig
Moses, Robb
author_sort Hejna, James
collection PubMed
description 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.
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spelling pubmed-20940912007-12-03 The hSNM1 protein is a DNA 5′-exonuclease Hejna, James Philip, Sahaayaruban Ott, Jesse Faulkner, Craig Moses, Robb Nucleic Acids Res Nucleic Acid Enzymes 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. Oxford University Press 2007-09 2007-09-05 /pmc/articles/PMC2094091/ /pubmed/17804464 http://dx.doi.org/10.1093/nar/gkm530 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ 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.
spellingShingle Nucleic Acid Enzymes
Hejna, James
Philip, Sahaayaruban
Ott, Jesse
Faulkner, Craig
Moses, Robb
The hSNM1 protein is a DNA 5′-exonuclease
title The hSNM1 protein is a DNA 5′-exonuclease
title_full The hSNM1 protein is a DNA 5′-exonuclease
title_fullStr The hSNM1 protein is a DNA 5′-exonuclease
title_full_unstemmed The hSNM1 protein is a DNA 5′-exonuclease
title_short The hSNM1 protein is a DNA 5′-exonuclease
title_sort hsnm1 protein is a dna 5′-exonuclease
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2094091/
https://www.ncbi.nlm.nih.gov/pubmed/17804464
http://dx.doi.org/10.1093/nar/gkm530
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