Publication Information
Puyaubert et al., 2014
No external accession available
Abstract
Plant Sci. 2014 Feb;215-216:150-6. doi: 10.1016/j.plantsci.2013.10.014. Epub
2013 Nov 1.
Identification of endogenously S-nitrosylated proteins in Arabidopsis plantlets:
effect of cold stress on cysteine nitrosylation level.
Puyaubert J(1), Fares A(2), Rézé N(3), Peltier JB(2), Baudouin E(3).
Author information:
(1)UPMC Univ Paris 06, UR 5, Laboratoire de Physiologie Cellulaire et
Moléculaire des Plantes, F-75005 Paris, France; CNRS, EAC 7180, Laboratoire de
Physiologie Cellulaire et Moléculaire des Plantes, F-75005 Paris, France.
Electronic address: juliette.puyaubert@upmc.fr.
(2)INRA, UR1199, Laboratoire de Protéomique Fonctionnelle, 34060 Montpellier
Cedex, France.
(3)UPMC Univ Paris 06, UR 5, Laboratoire de Physiologie Cellulaire et
Moléculaire des Plantes, F-75005 Paris, France; CNRS, EAC 7180, Laboratoire de
Physiologie Cellulaire et Moléculaire des Plantes, F-75005 Paris, France.
S-nitrosylation is a nitric oxide (NO)-based post-translational modification
regulating protein function and signalling. We used a combination between the
biotin switch method and labelling with isotope-coded affinity tag to identify
endogenously S-nitrosylated peptides in Arabidopsis thaliana proteins extracted
from plantlets. The relative level of S-nitrosylation in the identified peptides
was compared between unstressed and cold-stress seedlings. We thereby detected
62 endogenously nitrosylated peptides out of which 20 are over-nitrosylated
following cold exposure. Taken together these data provide a new repertoire of
endogenously S-nitrosylated proteins in Arabidopsis with cysteine
S-nitrosylation site. Furthermore they highlight the quantitative modification
of the S-nitrosylation status of specific cysteine following cold stress.
Copyright © 2013 Elsevier Ireland Ltd. All rights reserved.
DOI: 10.1016/j.plantsci.2013.10.014
PMID: 24388526 [Indexed for MEDLINE]
