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dc.contributor.authorDe Souza, Gustavo Antonioeng
dc.contributor.authorLeversen, Nils Anderseng
dc.contributor.authorMålen, Hiwaeng
dc.contributor.authorWiker, Harald Geng
dc.date.accessioned2015-04-14T12:20:45Z
dc.date.available2015-04-14T12:20:45Z
dc.date.issued2011-12-21eng
dc.identifier.issn1874-3919en_US
dc.identifier.issn1876-7737en_US
dc.identifier.urihttps://hdl.handle.net/1956/9779
dc.description.abstractCorrect protein compartmentalization is a key step for molecular function and cell viability, and this is especially true for membrane and externalized proteins of bacteria. Recent proteomic reports of Bacillus subtilis have shown that many proteins with Sec-like signal peptides and absence of a transmembrane helix domain are still observed in membrane-enriched fractions, but further evidence about signal peptide cleavage or soluble protein contamination is still needed. Here we report a proteomic screening of identified peptides in culture filtrate, membrane fraction and whole cell lysate of Mycobacterium tuberculosis. We were able to detect peptide sequencing evidence that shows that the predicted signal peptide was kept uncleaved for several types of proteins such as mammalian cell entry (Mce) proteins and PE or PE-PGRS proteins. Label-free quantitation of all proteins identified in each fraction showed that the majority of these proteins with uncleaved signal peptides are, indeed, enriched in the Triton X-114 lipid phase. Some of these proteins are likely to be located in the inner membrane while others may be outer membrane proteins.en_US
dc.language.isoengeng
dc.publisherElsevieren_US
dc.relation.urihttp://www.sciencedirect.com/science/article/pii/S1874391911004313eng
dc.rightsAttribution-NonCommercial-NoDerivs CC BY-NC-NDeng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/eng
dc.subjectMycobacterium tuberculosiseng
dc.subjectMammalian cell entry proteinseng
dc.subjectMass spectrometryeng
dc.subjectMembrane proteinseng
dc.subjectSecreted proteinseng
dc.subjectSignal peptideseng
dc.subjectSignalpeptidernob
dc.titleBacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathwayen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2015-04-01T07:02:21Zen_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2011 Elsevier B.V. Open access under CC BY-NC-ND license.en_US
dc.identifier.doihttps://doi.org/10.1016/j.jprot.2011.08.016
dc.identifier.cristin840618
dc.source.journalJournal of Proteomics
dc.source.4075
dc.source.142
dc.source.pagenumber502-510
dc.subject.nsiVDP::Medical sciences: 700::Basic medical, dental and veterinary sciences: 710::Medical microbiology: 715en_US
dc.subject.nsiVDP::Medisinske fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk mikrobiologi : 715nob


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