Structural basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity
The Phospholipase D (PLD) superfamily of proteins includes a group of enzymes with nuclease activity on various nucleic acid substrates. Here, with the aim of better understanding the substrate specificity determinants in this subfamily, we have characterised the enzymatic activity and the crystal s...
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| Veröffentlicht in: | PloS one 2017-12, Vol.12 (12), p.e0189049-e0189049 |
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| creator | Celma, Louisa Corbinais, Christopher Vercruyssen, Julien Veaute, Xavier de la Sierra-Gallay, Inès Li Guérois, Raphaël Busso, Didier Mathieu, Aurélie Marsin, Stéphanie Quevillon-Cheruel, Sophie Radicella, J Pablo |
| description | The Phospholipase D (PLD) superfamily of proteins includes a group of enzymes with nuclease activity on various nucleic acid substrates. Here, with the aim of better understanding the substrate specificity determinants in this subfamily, we have characterised the enzymatic activity and the crystal structure of NucT, a nuclease implicated in Helicobacter pylori purine salvage and natural transformation and compared them to those of its bacterial and mammalian homologues. NucT exhibits an endonuclease activity with a strong preference for single stranded nucleic acids substrates. We identified histidine124 as essential for the catalytic activity of the protein. Comparison of the NucT crystal structure at 1.58 Å resolution reported here with those of other members of the sub-family suggests that the specificity of NucT for single-stranded nucleic acids is provided by the width of a positively charged groove giving access to the catalytic site. |
| doi_str_mv | 10.1371/journal.pone.0189049 |
| format | Article |
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Comparison of the NucT crystal structure at 1.58 Å resolution reported here with those of other members of the sub-family suggests that the specificity of NucT for single-stranded nucleic acids is provided by the width of a positively charged groove giving access to the catalytic site.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0189049</identifier><identifier>PMID: 29206236</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Bacteria ; Bioinformatics ; Biology ; Biology and life sciences ; Catalysis ; Catalytic activity ; Crystal structure ; Deoxyribonucleic acid ; DNA ; Drug resistance ; Endonuclease ; Enzymatic activity ; Enzymes ; Helicobacter pylori ; Homology ; Life Sciences ; Medicine and Health Sciences ; Nuclease ; Nucleic acids ; Phospholipase ; Phospholipase D ; Phospholipases ; Physical sciences ; Proteins ; Salvage ; Selectivity ; Signal transduction ; Substrate specificity ; Substrates ; Transformation</subject><ispartof>PloS one, 2017-12, Vol.12 (12), p.e0189049-e0189049</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Celma et al. 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Here, with the aim of better understanding the substrate specificity determinants in this subfamily, we have characterised the enzymatic activity and the crystal structure of NucT, a nuclease implicated in Helicobacter pylori purine salvage and natural transformation and compared them to those of its bacterial and mammalian homologues. NucT exhibits an endonuclease activity with a strong preference for single stranded nucleic acids substrates. We identified histidine124 as essential for the catalytic activity of the protein. 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basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity</title><author>Celma, Louisa ; Corbinais, Christopher ; Vercruyssen, Julien ; Veaute, Xavier ; de la Sierra-Gallay, Inès Li ; Guérois, Raphaël ; Busso, Didier ; Mathieu, Aurélie ; Marsin, Stéphanie ; Quevillon-Cheruel, Sophie ; Radicella, J Pablo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c792t-adc637abdb0960c03946b0663037d166e81296fb79159e29d368af448f416f783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Bacteria</topic><topic>Bioinformatics</topic><topic>Biology</topic><topic>Biology and life sciences</topic><topic>Catalysis</topic><topic>Catalytic activity</topic><topic>Crystal structure</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Drug resistance</topic><topic>Endonuclease</topic><topic>Enzymatic activity</topic><topic>Enzymes</topic><topic>Helicobacter 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Aurélie</au><au>Marsin, Stéphanie</au><au>Quevillon-Cheruel, Sophie</au><au>Radicella, J Pablo</au><au>Gonzalez-Bello, Concepción</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-12-04</date><risdate>2017</risdate><volume>12</volume><issue>12</issue><spage>e0189049</spage><epage>e0189049</epage><pages>e0189049-e0189049</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The Phospholipase D (PLD) superfamily of proteins includes a group of enzymes with nuclease activity on various nucleic acid substrates. Here, with the aim of better understanding the substrate specificity determinants in this subfamily, we have characterised the enzymatic activity and the crystal structure of NucT, a nuclease implicated in Helicobacter pylori purine salvage and natural transformation and compared them to those of its bacterial and mammalian homologues. NucT exhibits an endonuclease activity with a strong preference for single stranded nucleic acids substrates. We identified histidine124 as essential for the catalytic activity of the protein. Comparison of the NucT crystal structure at 1.58 Å resolution reported here with those of other members of the sub-family suggests that the specificity of NucT for single-stranded nucleic acids is provided by the width of a positively charged groove giving access to the catalytic site.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29206236</pmid><doi>10.1371/journal.pone.0189049</doi><tpages>e0189049</tpages><orcidid>https://orcid.org/0000-0002-8807-7226</orcidid><orcidid>https://orcid.org/0000-0002-6473-8915</orcidid><orcidid>https://orcid.org/0000-0003-3027-7900</orcidid><orcidid>https://orcid.org/0000-0001-5294-2858</orcidid><orcidid>https://orcid.org/0000-0003-4868-247X</orcidid><orcidid>https://orcid.org/0000-0002-7074-7818</orcidid><oa>free_for_read</oa></addata></record> |
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| source | DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Bacteria Bioinformatics Biology Biology and life sciences Catalysis Catalytic activity Crystal structure Deoxyribonucleic acid DNA Drug resistance Endonuclease Enzymatic activity Enzymes Helicobacter pylori Homology Life Sciences Medicine and Health Sciences Nuclease Nucleic acids Phospholipase Phospholipase D Phospholipases Physical sciences Proteins Salvage Selectivity Signal transduction Substrate specificity Substrates Transformation |
| title | Structural basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity |
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