Proteomics

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Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites


ABSTRACT: Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of peptide-centric chemoproteomics, 1,537 S-sulfenylated sites were mapped on more than 1,000 proteins in Arabidopsis thaliana cells. The H2O2 sensitivity was quantified of more than 70% of these endogenous oxidation events toward exogenous H2O2 stimulation. Proteins involved in RNA and metabolic processing were identified as hotspots for S-sulfenylation. Moreover, S-sulfenylation frequently occurred on cysteines located in catalytic sites of enzymes or on cysteines involved in metal binding, hinting at direct mode-of-actions for redox regulation. Comparison of human and Arabidopsis S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the Arabidopsis MITOGEN-ACTIVATED PROTEIN KINASE4 (AtMAPK4) that corresponds to Cys161 in the human MAPK1, which is speculated to be a redox-regulatory site. Replacement of the noncatalytic Cys181 of the recombinant AtMAPK4 by the redox-insensitive serine decreased the protein kinase activity, emphasizing the importance of this noncatalytic cysteine. Altogether, we quantitatively mapped the S-sulfenylated cysteines in Arabidopsis plants under oxidative stress and delivered an unprecedented inventory for unraveling the precise role of these oxidized cysteines in plant redox signaling.

INSTRUMENT(S): Orbitrap Fusion

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

TISSUE(S): Plant Cell

SUBMITTER: Jing Yang  

LAB HEAD: Jing Yang

PROVIDER: PXD013495 | Pride | 2019-09-16

REPOSITORIES: Pride

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Publications

Mining for protein S-sulfenylation in <i>Arabidopsis</i> uncovers redox-sensitive sites.

Huang Jingjing J   Willems Patrick P   Wei Bo B   Tian Caiping C   Ferreira Renan B RB   Bodra Nandita N   Martínez Gache Santiago Agustín SA   Wahni Khadija K   Liu Keke K   Vertommen Didier D   Gevaert Kris K   Carroll Kate S KS   Van Montagu Marc M   Yang Jing J   Van Breusegem Frank F   Messens Joris J  

Proceedings of the National Academy of Sciences of the United States of America 20191002 42


Hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) is an important messenger molecule for diverse cellular processes. H<sub>2</sub>O<sub>2</sub> oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of a peptide-centric chemoproteomics approach, we  ...[more]

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