Dataset Information

Comparative quantitative proteomic analysis of Arabidopsis thylakoid membranes from plants grown under low, moderate and high illumination. Effects of stn7 and tap38 mutations.

ABSTRACT: Plants grown under different illumination levels undergo a long-term acclimation response (LTR) resulting in differences in their leaf morphology and chloroplast protein composition to maximise their growth. At the proteomic level, LTR involves modulating the stoichiometry of photosynthetic complexes within the thylakoid membrane through de novo synthesis and degradation of specific proteins. The signalling pathways that mediate LTR in relation to light intensity remain largely unknown, however earlier studies demonstrated a key role for the light-harvesting complex II (LHCII) serine-threonine kinase STN7. We explored the effects of mutant strains of Arabidopsis targeting STN7 and its cognate phosphatase TAP38 in the LTR to low, moderate and high illumination, employing label-free quantitative proteomic analysis.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell

SUBMITTER: Philip Jackson

LAB HEAD: Matt Johnson

PROVIDER: PXD037358 | Pride | 2023-03-30

REPOSITORIES: Pride

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			Action	DRS
	20200129_SF_Ara_HL_Stn7_1a.raw	Raw
	20200129_SF_Ara_HL_Stn7_1b-001.raw	Raw
	20200129_SF_Ara_HL_Stn7_1c-023.raw	Raw
	20200129_SF_Ara_HL_Stn7_2a-016.raw	Raw
	20200129_SF_Ara_HL_Stn7_2b-007.raw	Raw

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Project description:Cysteine occupies a central position in plant metabolism due to its biochemical functions. Arabidopsis thaliana cells contain different O-acetylserine(thiol)lyase (OASTL) enzymes that catalyze the biosynthesis of cysteine. Because they are localized in the cytosol, plastids and mitochondria, this results in multiple subcellular cysteine pools. Much progress has been made on the most abundant OASTL enzymes; however, information on the less abundant OASTL-like proteins has been scarce. To unequivocally establish the enzymatic reaction catalyzed by the minor cytosolic OASTL isoform CS-LIKE (AT5G28030), we expressed this enzyme in bacteria and characterized the purified recombinant protein. Our results demonstrate that CS-LIKE catalyzes the desulfuration of L-cysteine to sulfide plus ammonia and pyruvate. Thus, CS-LIKE is a novel L-cysteine desulfhydrase (EC 4.4.1.1), and we propose to designate it DES1. The impact and functionality of DES1 in cysteine metabolism was revealed by the phenotype of the T-DNA insertion mutants des1-1 and des1-2. Mutation of the DES1 gene leads to premature leaf senescence, as demonstrated by the increased expression of senescence-associated genes and transcription factors. Also, the absence of DES1 significantly reduces the total cysteine desulfuration activity in leaves, and there is a concomitant increase in the total cysteine content. As a consequence, the expression levels of sulfur-responsive genes are de-regulated, and the mutant plants show enhanced antioxidant defenses and tolerance to conditions that promote oxidative stress. Our results suggest that DES1 from Arabidopsis is an L-cysteine desulfhydrase involved in maintaining cysteine homeostasis, mainly at late developmental stages or under environmental perturbations. Using the Affymetrix ATH1 GeneChips, we performed a comparative transcriptomic analysis on leaves of the des1-1 and wild type plants grown on soil for three weeks. Three biological replicates were performed for each sample and hybridized to the chips. We made the comparison of des1-1 leaves versus wild-type leaves to classify the differently expressed genes in the mutant plant.

Dataset Information

Comparative quantitative proteomic analysis of Arabidopsis thylakoid membranes from plants grown under low, moderate and high illumination. Effects of stn7 and tap38 mutations.

Dataset's files

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