Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins
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Parrott, Brian Jonathan
Jankovic, Boris R.
Lilley, Kathryn S
Gehring, Christoph A
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Bioscience Core Lab
Chemical Engineering Program
Computational Bioscience Research Center (CBRC)
Molecular Signalling Group
Online Publication Date2013-01-05
Print Publication Date2013
Permanent link to this recordhttp://hdl.handle.net/10754/325257
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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.
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.
JournalCell Communication and Signaling
PubMed Central IDPMC3544604
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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.
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- Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins.
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- Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II.
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- redox Signaling by 8-nitro-cyclic guanosine monophosphate: nitric oxide- and reactive oxygen species-derived electrophilic messenger.
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- Authors: Anbanandam A, Bieber Urbauer RJ, Bartlett RK, Smallwood HS, Squier TC, Urbauer JL
- Issue date: 2005 Jul 12
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