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Abstract
Biochem Biophys Res Commun. 2011 Dec 16;416(3-4):331-6. doi:
10.1016/j.bbrc.2011.11.036. Epub 2011 Nov 15.
Proteomics investigation of endogenous S-nitrosylation in Arabidopsis.
Fares A(1), Rossignol M, Peltier JB.
Author information:
(1)INRA, UR1199, Laboratoire de Protéomique Fonctionnelle, 34060 Montpellier
Cedex, France.
S-Nitrosylation emerges as an important protein modification in many processes.
However, most data were obtained at the protein level after addition of a NO
donor, particularly in plants where information about the cysteines nitrosylated
in these proteins is scarce. An adapted work-flow, combining the classical
biotin switch method and labeling with isotope-coded affinity tags (ICAT), is
proposed. Without addition of NO donor, a total of 53 endogenous
nitrosocysteines was identified in Arabidopsis cells, in proteins belonging to
all cell territories, including membranes, and covering a large panel of
functions. This first repertoire of nitrosothiols in plants enabled also
preliminary structural description. Three apolar motifs, not located in close
vicinity of cysteines and accounting for half the dataset, were detected and are
proposed to complement nitrosylation prediction algorithms, poorly trained with
plant data to date. Analysis of changes induced by a brief salt stress showed
that NaCl modified the nitrosylation level of a small proportion of endogenously
nitrosylated proteins and did not concern all nitrosothiols in these proteins.
The possible role of some NO targets in the response to salt stress was
discussed.
Copyright © 2011 Elsevier Inc. All rights reserved.
DOI: 10.1016/j.bbrc.2011.11.036
PMID: 22115780 [Indexed for MEDLINE]
