Dataset Information

Cysteine thiol trioxidation induce aging

ABSTRACT: LC-MS/MS proteomic method is used to coduct skin and lungs proteomics profiling. Many protein with cysteine thiol trioxidation were identified in tissues of old mice. the modified proteins are predicted to induce celllular aging.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Skin

SUBMITTER: SoFong Cam Ngan

LAB HEAD: Newman Sze

PROVIDER: PXD037908 | Pride | 2024-05-22

REPOSITORIES: Pride

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Publications

Trioxidized cysteine in the aging proteome mimics the structural dynamics and interactome of phosphorylated serine.

Sánchez Milán Jose Antonio JA Fernández-Rhodes María M Guo Xue X Mulet María M Ngan SoFong Cam SC Iyappan Ranjith R Katoueezadeh Maryam M Sze Siu Kwan SK Serra Aida A Gallart-Palau Xavier X

Aging cell 20231218 3

Aging is the primary risk factor for the development of numerous human chronic diseases. On a molecular level, it significantly impacts the regulation of protein modifications, leading to the accumulation of degenerative protein modifications (DPMs) such as aberrant serine phosphorylation (p-Ser) and trioxidized cysteine (t-Cys) within the proteome. The altered p-Ser is linked to abnormal cell signaling, while the accumulation of t-Cys is associated with chronic diseases induced by oxidative str ...[more]

PMID: 38111315

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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.

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	181119_SKIN_M_24_01A.raw	Raw
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	181119_SKIN_M_24_01C.raw	Raw
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	181119_SKIN_M_24_02B.raw	Raw