Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/24736
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dc.contributor.authorMatallana-Surget, Sabine-
dc.contributor.authorCavicchioli, Rick-
dc.contributor.authorFauconnier, Charles-
dc.contributor.authorWattiez, Ruddy-
dc.contributor.authorBaptiste, Leroy-
dc.contributor.authorJoux, Fabien-
dc.contributor.authorRaftery, Mark-
dc.contributor.authorLebaron, Philippe-
dc.date.accessioned2017-08-12T01:53:38Z-
dc.date.available2017-08-12T01:53:38Z-
dc.date.issued2013-07-09-
dc.identifier.othere68112-
dc.identifier.urihttp://hdl.handle.net/1893/24736-
dc.description.abstractUVB oxidizes proteins through the generation of reactive oxygen species. One consequence of UVB irradiation is carbonylation, the irreversible formation of a carbonyl group on proline, lysine, arginine or threonine residues. In this study, redox proteomics was performed to identify carbonylated proteins in the UVB resistant marine bacterium Photobacterium angustum. Mass-spectrometry was performed with either biotin-labeled or dinitrophenylhydrazide (DNPH) derivatized proteins. The DNPH redox proteomics method enabled the identification of 62 carbonylated proteins (5% of 1221 identified proteins) in cells exposed to UVB or darkness. Eleven carbonylated proteins were quantified and the UVB/dark abundance ratio was determined at both the protein and peptide levels. As a result we determined which functional classes of proteins were carbonylated, which residues were preferentially modified, and what the implications of the carbonylation were for protein function. As the first large scale, shotgun redox proteomics analysis examining carbonylation to be performed on bacteria, our study provides a new level of understanding about the effects of UVB on cellular proteins, and provides a methodology for advancing studies in other biological systems.en_UK
dc.language.isoen-
dc.publisherPublic Library of Science-
dc.relationMatallana-Surget S, Cavicchioli R, Fauconnier C, Wattiez R, Baptiste L, Joux F, Raftery M & Lebaron P (2013) Shotgun redox proteomics: identification and quantitation of carbonylated proteins in the UVB resistant marine bacterium, Photobacterium angustum S14, PLoS ONE, 8 (7), Art. No.: e68112.-
dc.rights© 2013 Matallana-Surget et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.-
dc.titleShotgun redox proteomics: identification and quantitation of carbonylated proteins in the UVB resistant marine bacterium, Photobacterium angustum S14en_UK
dc.typeJournal Articleen_UK
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0068112-
dc.identifier.pmid23874515-
dc.citation.jtitlePLoS ONE-
dc.citation.issn1932-6203-
dc.citation.volume8-
dc.citation.issue7-
dc.citation.publicationstatusPublished-
dc.citation.peerreviewedRefereed-
dc.type.statusPublisher version (final published refereed version)-
dc.author.emailsabine.matallanasurget@stir.ac.uk-
dc.citation.date09/07/2013-
dc.contributor.affiliationBiological and Environmental Sciences-
dc.contributor.affiliationUniversity of New South Wales-
dc.contributor.affiliationUniversity of Paris 6 (Pierre and Marie Curie University)-
dc.contributor.affiliationUniversity of Mons-
dc.contributor.affiliationUniversity of Mons-
dc.contributor.affiliationUniversity of Paris 6 (Pierre and Marie Curie University)-
dc.contributor.affiliationUniversity of New South Wales-
dc.contributor.affiliationUniversity of Paris 6 (Pierre and Marie Curie University)-
dc.identifier.isi000321736900059-
Appears in Collections:Biological and Environmental Sciences Journal Articles

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