Proteomics

Dataset Information

0

Identification of the S-sulfenylated residues of GSNOR1 in Arabidopsis


ABSTRACT: The major mechanism by which H2O2 executes its physiological functions is through oxidation of sulfur in the target proteins. Thiol groups of protein cysteine (Cys) could be oxidized by H2O2 to sulfenic, a process also known as S-sulfenylation. Therefore, we reasoned that the activity of GSNOR1 might be regulated by H2O2 through S-sulfenylation. An in vitro S-sulfenylation assay revealed that GSNOR1-His recombinant protein was S-sulfenylated. Because Cys-284 and Cys-285 of GSNOR1 are adjacent and located on the same enzymolysis peptide segment, and also because both of them were identified as S-sulfenylated residues in vivo, to further test whether Cys-284 is S-sulfenylated, Cys-285 was substituted with serine (Ser).

INSTRUMENT(S): LTQ Orbitrap Elite

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

TISSUE(S): Cell Culture

SUBMITTER: Hongyan Guo  

LAB HEAD: Jianru Zuo

PROVIDER: PXD056375 | Pride | 2025-01-23

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
ZJR_SSN_G1_3_20201113.raw Raw
ZJR_SSN_G1_3_20201113.xlsx Xlsx
ZJR_SSN_GSNOR1_C285S_ELITE_20221104.raw Raw
ZJR_SSN_GSNOR1_C285S_ELITE_20221104.xlsx Xlsx
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