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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/182977
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dc.contributor.authorChoi, Han-Pil-
dc.contributor.authorJuárez, Silvia-
dc.contributor.authorCiordia, Sergio-
dc.contributor.authorFernández, Marisol-
dc.contributor.authorBargiela, Rafael-
dc.contributor.authorAlbar, Juan Pablo-
dc.contributor.authorMazumdar, Varun-
dc.contributor.authorAnton, Brian P.-
dc.contributor.authorKasif, Simon-
dc.contributor.authorFerrer, Manuel-
dc.contributor.authorSteffen, Martin-
dc.date.accessioned2019-05-31T06:57:56Z-
dc.date.available2019-05-31T06:57:56Z-
dc.date.issued2013-06-18-
dc.identifier.citationPlos One 8(6): e66605 (2013)-
dc.identifier.issn1932-6203-
dc.identifier.urihttp://hdl.handle.net/10261/182977-
dc.description© 2013 Choi et al.-
dc.description.abstractThe functional characterization of Open Reading Frames (ORFs) from sequenced genomes remains a bottleneck in our effort to understand microbial biology. In particular, the functional characterization of proteins with only remote sequence homology to known proteins can be challenging, as there may be few clues to guide initial experiments. Affinity enrichment of proteins from cell lysates, and a global perspective of protein function as provided by COMBREX, affords an approach to this problem. We present here the biochemical analysis of six proteins from Helicobacter pylori ATCC 26695, a focus organism in COMBREX. Initial hypotheses were based upon affinity capture of proteins from total cellular lysate using derivatized nano-particles, and subsequent identification by mass spectrometry. Candidate genes encoding these proteins were cloned and expressed in Escherichia coli, and the recombinant proteins were purified and characterized biochemically and their biochemical parameters compared with the native ones. These proteins include a guanosine triphosphate (GTP) cyclohydrolase (HP0959), an ATPase (HP1079), an adenosine deaminase (HP0267), a phosphodiesterase (HP1042), an aminopeptidase (HP1037), and new substrates were characterized for a peptidoglycan deacetylase (HP0310). Generally, characterized enzymes were active at acidic to neutral pH (4.0–7.5) with temperature optima ranging from 35 to 55°C, although some exhibited outstanding characteristics.-
dc.description.sponsorshipThe cloning and biochemical testing of recombinant proteins was funded by RC2-GM092602 from the National Institutes of Health (NIGMS), awarded to COMBREX (SK, MS). Affinity enrichment and testing of native proteins was funded by the Spanish Ministry of Economy and Competitiveness (former MICINN), within the ERA NET PathoGenoMics2 call, grant number 0315441A and BFU2008-04501-E/BMC (MF).-
dc.publisherPublic Library of Science-
dc.relation.isversionofPublisher's version-
dc.rightsopenAccess-
dc.titleBiochemical Characterization of Hypothetical Proteins from Helicobacter pylori-
dc.typeartículo-
dc.identifier.doi10.1371/journal.pone.0066605-
dc.relation.publisherversionhttps://doi.org/10.1371/journal.pone.0066605-
dc.date.updated2019-05-31T06:57:56Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.rights.licensehttps://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.contributor.funderMinisterio de Ciencia e Innovación (España)-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderNational Institutes of Health (US)-
dc.relation.csicSí-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100004837es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100000002es_ES
dc.identifier.pmid23825549-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.cerifentitytypePublications-
item.openairetypeartículo-
item.grantfulltextopen-
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