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Nitrogen deprivation Ph response

Phosphorylation in Arabidopsis thaliana

27 modifications in 21 peptides, found in 69 proteins

Experiment Details

Exp 39


Experimental Setup
TissueSeedlings
ConditionNitrate starvation and resupply
PTM EnrichmentTi-IMAC
MS InstrumentLTQ
MS/MS Search Parameters
Protein DatabaseTAIR10
Decoy StrategyReverse decoy database
FDR ThresholdPeptide 1%
Search Algorithm(s)SEQUEST
Precursor Mass Tolerance50 ppm
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsOxidation (M)
Phosphorylation (STY)
Other Information
CommentsPhosphat 4.0 - Defined sites (pS/T/Y).


Publication Information

Wang et al., 2012

PubMed ID: 22329444

No external accession available

Abstract

J Proteome Res. 2012 Apr 6;11(4):2301-15. doi: 10.1021/pr2010764. Epub 2012 Feb 
29.

A comprehensive differential proteomic study of nitrate deprivation in 
Arabidopsis reveals complex regulatory networks of plant nitrogen responses.

Wang X(1), Bian Y, Cheng K, Zou H, Sun SS, He JX.

Author information:
(1)School of Life Sciences, Tsinghua University, Beijing 100084, China.

Nitrogen (N) is an important nutrient and signal for plant growth and 
development. However, to date, our knowledge of how plants sense and transduce 
the N signals is very limited. To better understand the molecular mechanisms of 
plant N responses, we took two-dimensional gel-based proteomic and 
phosphoproteomic approaches to profile the proteins with abundance and 
phosphorylation state changes during nitrate deprivation and recovery in the 
model plant Arabidopsis thaliana. After 7-day-old seedlings were N-deprived for 
up to 48 h followed by 24 h recovery, a total of 170 and 38 proteins were 
identified with significant changes in abundance and phosphorylation state, 
respectively. Bioinformatic analyses implicate these proteins in diverse 
cellular processes including N and protein metabolisms, photosynthesis, 
cytoskeleton, redox homeostasis, and signal transduction. Functional studies of 
the selected nitrate-responsive proteins indicate that the proteasome regulatory 
subunit RPT5a and the cytoskeleton protein Tubulin alpha-6 (TUA6) play important 
roles in plant nitrate responses by regulating plant N use efficiency (NUE) and 
low nitrate-induced anthocyanin biosynthesis, respectively. In conclusion, our 
study provides novel insights into plant responses to nitrate at the proteome 
level, which are expected to be highly useful for dissecting the N response 
pathways in higher plants and for improving plant NUE.

DOI: 10.1021/pr2010764
PMID: 22329444 [Indexed for MEDLINE]