Registro completo de metadatos
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.creator | O'Rourke, Eyleen J. | - |
dc.creator | Chevalier, Catherine | - |
dc.creator | Boiteux, Serge | - |
dc.creator | Labigne, Agnès | - |
dc.creator | Ielpi, Luis | - |
dc.creator | Radicella, Juan Pablo | - |
dc.date | 2018-05-15T19:09:42Z | - |
dc.date | 2018-05-15T19:09:42Z | - |
dc.date | 2000-06 | - |
dc.date | 2018-05-10T15:45:32Z | - |
dc.date.accessioned | 2019-04-29T15:53:31Z | - |
dc.date.available | 2019-04-29T15:53:31Z | - |
dc.date.issued | 2000-06 | - |
dc.identifier | O'Rourke, Eyleen J.; Chevalier, Catherine; Boiteux, Serge; Labigne, Agnès; Ielpi, Luis; et al.; A Novel 3-Methyladenine DNA Glycosylase from Helicobacter pylori Defines a New Class within the Endonuclease III Family of Base Excision Repair Glycosylases; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 275; 26; 6-2000; 20077-20083 | - |
dc.identifier | 0021-9258 | - |
dc.identifier | http://hdl.handle.net/11336/45245 | - |
dc.identifier | 1083-351X | - |
dc.identifier | CONICET Digital | - |
dc.identifier | CONICET | - |
dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/304790 | - |
dc.description | The cloning, purification, and characterization of MagIII, a 3-methyladenine DNA glycosylase from Helicobacter pylori, is presented in this paper. Sequence analysis of the genome of this pathogen failed to identify open reading frames potentially coding for proteins with a 3-methyladenine DNA glycosylase activity. The putative product of the HP602 open reading frame, reported as an endonuclease III, shares extensive amino acid sequence homology with some bacterial members of this family and has the canonic active site helix-hairpin-helix-GPD motif. Surprisingly, this predicted H. pylori endonuclease III encodes a 25,220-Da protein able to release 3-methyladenine, but not oxidized bases, from modified DNA. MagIII has no abasic site lyase activity and displays the substrate specificity of the 3-methyladenine-DNA glycosylase type I of Escherichia coli (Tag) because it is not able to recognize 7-methylguanine or hypoxanthine as substrates. The expression of the magIII open reading frame in null 3-methyladenine glycosylase E. coli (tag alkA) restores to this mutant partial resistance to alkylating agents. MagIII-deficient H. pylori cells show an alkylation-sensitive phenotype. H. pylori wild type cells exposed to alkylating agents present an adaptive response by inducing the expression of magIII. MagIII is thus a novel bacterial member of the endonuclease III family, which displays biochemical properties not described for any of the members of this group until now. | - |
dc.description | Fil: O'Rourke, Eyleen J.. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina | - |
dc.description | Fil: Chevalier, Catherine. Instituto Pasteur; Francia | - |
dc.description | Fil: Boiteux, Serge. Centre National de la Recherche Scientifique; Francia | - |
dc.description | Fil: Labigne, Agnès. Instituto Pasteur; Francia | - |
dc.description | Fil: Ielpi, Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina | - |
dc.description | Fil: Radicella, Juan Pablo. Centre National de la Recherche Scientifique; Francia | - |
dc.format | application/pdf | - |
dc.format | application/pdf | - |
dc.language | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/275/26/20077.long | - |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M001071200 | - |
dc.rights | info:eu-repo/semantics/openAccess | - |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
dc.source | reponame:CONICET Digital (CONICET) | - |
dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
dc.source | instacron:CONICET | - |
dc.subject | HELICOBACTER PYLORI | - |
dc.subject | Otras Ciencias Biológicas | - |
dc.subject | Ciencias Biológicas | - |
dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
dc.title | A Novel 3-Methyladenine DNA Glycosylase from Helicobacter pylori Defines a New Class within the Endonuclease III Family of Base Excision Repair Glycosylases | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.type | info:ar-repo/semantics/articulo | - |
Aparece en las colecciones: | CONICET |
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