Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins

Handle URI:
http://hdl.handle.net/10754/325257
Title:
Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins
Authors:
Marondedze, Claudius ( 0000-0002-2113-904X ) ; Turek, Ilona ( 0000-0001-6457-7456 ) ; Parrott, Brian Jonathan; Thomas, Ludivine; Jankovic, Boris R.; Lilley, Kathryn S; Gehring, Christoph A. ( 0000-0003-4355-4591 )
Abstract:
Background: 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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Computational Bioscience Research Center (CBRC)
Citation:
Marondedze 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.
Publisher:
Springer Nature
Journal:
Cell Communication and Signaling
Issue Date:
5-Jan-2013
DOI:
10.1186/1478-811X-11-1
PubMed ID:
23289948
PubMed Central ID:
PMC3544604
Type:
Article
ISSN:
1478811X
Appears in Collections:
Articles; Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorMarondedze, Claudiusen
dc.contributor.authorTurek, Ilonaen
dc.contributor.authorParrott, Brian Jonathanen
dc.contributor.authorThomas, Ludivineen
dc.contributor.authorJankovic, Boris R.en
dc.contributor.authorLilley, Kathryn Sen
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2014-08-27T09:42:54Z-
dc.date.available2014-08-27T09:42:54Z-
dc.date.issued2013-01-05en
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.en
dc.identifier.issn1478811Xen
dc.identifier.pmid23289948en
dc.identifier.doi10.1186/1478-811X-11-1en
dc.identifier.urihttp://hdl.handle.net/10754/325257en
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.en
dc.language.isoenen
dc.publisherSpringer Natureen
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.en
dc.rights.urihttp://creativecommons.org/licenses/by/2.0en
dc.subject3,5-cyclic guanosine monophosphateen
dc.subjectArabidopsis thalianaen
dc.subjectMethionine oxidationen
dc.subjectReactive oxygen speciesen
dc.subjectTandem mass spectrometry-based proteomicsen
dc.subject8 bromo cyclic GMPen
dc.subjectArabidopsis proteinen
dc.subjectheat shock proteinen
dc.subjectmethionineen
dc.subjectamino acid metabolismen
dc.subjectamino terminal sequenceen
dc.subjectArabidopsisen
dc.subjectcarboxy terminal sequenceen
dc.subjectcontrolled studyen
dc.subjectoxidation kineticsen
dc.subjectplant cellen
dc.subjectprotein functionen
dc.subjectprotein structureen
dc.subjectproteomicsen
dc.titleStructural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteinsen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.identifier.journalCell Communication and Signalingen
dc.identifier.pmcidPMC3544604en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDepartment of Biochemistry, Cambridge Systems Biology Centre, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, United Kingdomen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorMarondedze, Claudiusen
kaust.authorTurek, Ilonaen
kaust.authorParrott, Brian Jonathanen
kaust.authorThomas, Ludivineen
kaust.authorGehring, Christoph A.en
kaust.authorJankovic, Boris R.en
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