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dc.contributor.authorMarondedze, Claudius
dc.contributor.authorTurek, Ilona
dc.contributor.authorParrott, Brian Jonathan
dc.contributor.authorThomas, Ludivine
dc.contributor.authorJankovic, Boris R.
dc.contributor.authorLilley, Kathryn S
dc.contributor.authorGehring, Christoph A
dc.date.accessioned2014-08-27T09:42:54Z
dc.date.available2014-08-27T09:42:54Z
dc.date.issued2013-01-05
dc.identifier.citationMarondedze C, Turek I, Parrott B, Thomas L, Jankovic B, et al. (2013) Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins. Cell Communication and Signaling 11: 1. doi:10.1186/1478-811X-11-1.
dc.identifier.issn1478811X
dc.identifier.pmid23289948
dc.identifier.doi10.1186/1478-811X-11-1
dc.identifier.urihttp://hdl.handle.net/10754/325257
dc.description.abstractBackground: Increasing structural and biochemical evidence suggests that post-translational methionine oxidation of proteins is not just a result of cellular damage but may provide the cell with information on the cellular oxidative status. In addition, oxidation of methionine residues in key regulatory proteins, such as calmodulin, does influence cellular homeostasis. Previous findings also indicate that oxidation of methionine residues in signaling molecules may have a role in stress responses since these specific structural modifications can in turn change biological activities of proteins. Findings. Here we use tandem mass spectrometry-based proteomics to show that treatment of Arabidopsis thaliana cells with a non-oxidative signaling molecule, the cell-permeant second messenger analogue, 8-bromo-3,5-cyclic guanosine monophosphate (8-Br-cGMP), results in a time-dependent increase in the content of oxidised methionine residues. Interestingly, the group of proteins affected by cGMP-dependent methionine oxidation is functionally enriched for stress response proteins. Furthermore, we also noted distinct signatures in the frequency of amino acids flanking oxidised and un-oxidised methionine residues on both the C- and N-terminus. Conclusions: Given both a structural and functional bias in methionine oxidation events in response to a signaling molecule, we propose that these are indicative of a specific role of such post-translational modifications in the direct or indirect regulation of cellular responses. The mechanisms that determine the specificity of the modifications remain to be elucidated. 2013 Marondedze et al.; licensee BioMed Central Ltd.
dc.language.isoen
dc.publisherSpringer Nature
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rights.urihttp://creativecommons.org/licenses/by/2.0
dc.subject3,5-cyclic guanosine monophosphate
dc.subjectArabidopsis thaliana
dc.subjectMethionine oxidation
dc.subjectReactive oxygen species
dc.subjectTandem mass spectrometry-based proteomics
dc.subject8 bromo cyclic GMP
dc.subjectArabidopsis protein
dc.subjectheat shock protein
dc.subjectmethionine
dc.subjectamino acid metabolism
dc.subjectamino terminal sequence
dc.subjectArabidopsis
dc.subjectcarboxy terminal sequence
dc.subjectcontrolled study
dc.subjectoxidation kinetics
dc.subjectplant cell
dc.subjectprotein function
dc.subjectprotein structure
dc.subjectproteomics
dc.titleStructural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.identifier.journalCell Communication and Signaling
dc.identifier.pmcidPMC3544604
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDepartment of Biochemistry, Cambridge Systems Biology Centre, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, United Kingdom
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personMarondedze, Claudius
kaust.personTurek, Ilona
kaust.personParrott, Brian Jonathan
kaust.personThomas, Ludivine
kaust.personGehring, Christoph A
kaust.personJankovic, Boris R.
refterms.dateFOA2018-06-14T03:46:31Z


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This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.