Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/24736
Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Shotgun redox proteomics: identification and quantitation of carbonylated proteins in the UVB resistant marine bacterium, Photobacterium angustum S14
Authors: Matallana-Surget, Sabine
Cavicchioli, Rick
Fauconnier, Charles
Wattiez, Ruddy
Baptiste, Leroy
Joux, Fabien
Raftery, Mark
Lebaron, Philippe
Contact Email: sabine.matallanasurget@stir.ac.uk
Issue Date: 9-Jul-2013
Citation: Matallana-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.
Abstract: UVB 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.
DOI Link: http://dx.doi.org/10.1371/journal.pone.0068112
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.

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