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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...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2007
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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. |
format | Text |
id | pubmed-2094091 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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