Rules governing selective protein carbonylation.
BACKGROUND:Carbonyl derivatives are mainly formed by direct metal-catalysed oxidation (MCO) attacks on the amino-acid side chains of proline, arginine, lysine and threonine residues. For reasons unknown, only some proteins are prone to carbonylation. METHODOLOGY/PRINCIPAL FINDINGS:we used mass spect...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2009-10-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2751825?pdf=render |
| _version_ | 1798043199422332928 |
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| author | Etienne Maisonneuve Adrien Ducret Pierre Khoueiry Sabrina Lignon Sonia Longhi Emmanuel Talla Sam Dukan |
| author_facet | Etienne Maisonneuve Adrien Ducret Pierre Khoueiry Sabrina Lignon Sonia Longhi Emmanuel Talla Sam Dukan |
| author_sort | Etienne Maisonneuve |
| collection | DOAJ |
| description | BACKGROUND:Carbonyl derivatives are mainly formed by direct metal-catalysed oxidation (MCO) attacks on the amino-acid side chains of proline, arginine, lysine and threonine residues. For reasons unknown, only some proteins are prone to carbonylation. METHODOLOGY/PRINCIPAL FINDINGS:we used mass spectrometry analysis to identify carbonylated sites in: BSA that had undergone in vitro MCO, and 23 carbonylated proteins in Escherichia coli. The presence of a carbonylated site rendered the neighbouring carbonylatable site more prone to carbonylation. Most carbonylated sites were present within hot spots of carbonylation. These observations led us to suggest rules for identifying sites more prone to carbonylation. We used these rules to design an in silico model (available at http://www.lcb.cnrs-mrs.fr/CSPD/), allowing an effective and accurate prediction of sites and of proteins more prone to carbonylation in the E. coli proteome. CONCLUSIONS/SIGNIFICANCE:We observed that proteins evolve to either selectively maintain or lose predicted hot spots of carbonylation depending on their biological function. As our predictive model also allows efficient detection of carbonylated proteins in Bacillus subtilis, we believe that our model may be extended to direct MCO attacks in all organisms. |
| first_indexed | 2024-04-11T22:46:09Z |
| format | Article |
| id | doaj.art-5f5c86183910489e87d49354a3e55140 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-11T22:46:09Z |
| publishDate | 2009-10-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-5f5c86183910489e87d49354a3e551402022-12-22T03:58:44ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-10-01410e726910.1371/journal.pone.0007269Rules governing selective protein carbonylation.Etienne MaisonneuveAdrien DucretPierre KhoueirySabrina LignonSonia LonghiEmmanuel TallaSam DukanBACKGROUND:Carbonyl derivatives are mainly formed by direct metal-catalysed oxidation (MCO) attacks on the amino-acid side chains of proline, arginine, lysine and threonine residues. For reasons unknown, only some proteins are prone to carbonylation. METHODOLOGY/PRINCIPAL FINDINGS:we used mass spectrometry analysis to identify carbonylated sites in: BSA that had undergone in vitro MCO, and 23 carbonylated proteins in Escherichia coli. The presence of a carbonylated site rendered the neighbouring carbonylatable site more prone to carbonylation. Most carbonylated sites were present within hot spots of carbonylation. These observations led us to suggest rules for identifying sites more prone to carbonylation. We used these rules to design an in silico model (available at http://www.lcb.cnrs-mrs.fr/CSPD/), allowing an effective and accurate prediction of sites and of proteins more prone to carbonylation in the E. coli proteome. CONCLUSIONS/SIGNIFICANCE:We observed that proteins evolve to either selectively maintain or lose predicted hot spots of carbonylation depending on their biological function. As our predictive model also allows efficient detection of carbonylated proteins in Bacillus subtilis, we believe that our model may be extended to direct MCO attacks in all organisms.http://europepmc.org/articles/PMC2751825?pdf=render |
| spellingShingle | Etienne Maisonneuve Adrien Ducret Pierre Khoueiry Sabrina Lignon Sonia Longhi Emmanuel Talla Sam Dukan Rules governing selective protein carbonylation. PLoS ONE |
| title | Rules governing selective protein carbonylation. |
| title_full | Rules governing selective protein carbonylation. |
| title_fullStr | Rules governing selective protein carbonylation. |
| title_full_unstemmed | Rules governing selective protein carbonylation. |
| title_short | Rules governing selective protein carbonylation. |
| title_sort | rules governing selective protein carbonylation |
| url | http://europepmc.org/articles/PMC2751825?pdf=render |
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