Persulfidated subproteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes and nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in plants.

ABSTRACT: Hydrogen sulfide-mediated signaling pathways regulates many physiological andpathophysiological processes in mammalian and plant systems. The molecular mechanism bywhich hydrogen sulfide exerts its action involves the oxidative post-translational modificationof cysteine residues to form a persulfidated thiol motif, named as protein S-sulfhydration orpersulfidation. We have developed a comparative and quantitative proteomic analysisapproach for the detection of endogenous S-sulfhydrated proteins in wild-type Arabidopsisand L-CYSTEINE DESULFHYDRASE 1 mutant leaves by using the tag-switch method.Bioinformatic analysis of the identified proteins revealed that S-sulfhydrated cysteines arepart of a wide range of biological functions regulating important processes such as carbonmetabolism, plant responses to abiotic and biotic stresses, plant growth and development, andRNA translation. Quantitative analysis in both genetic backgrounds reveals hydrogen sulfidemediatedprotein sulfhydration as a new regulatory component in primary metabolic pathwayssuch as tricarboxylic acid cycle, glycolysis or Calvin cycle. In addition, studies on thesubcellular localization of glyceraldehyde-3-phosphate dehydrogenase show that sulfideregulates the cytosolic/nuclear partitioning by enhancing the nuclear localization of theprotein and appears to be a critical step for reprogramming cellular metabolism.

INSTRUMENT(S): TripleTOF 5600

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

SUBMITTER: Sergio Ciordia Higuera  

LAB HEAD: Luis C. Romero

PROVIDER: PXD005168 | Pride | 2017-10-27

REPOSITORIES: Pride