Proteomics

Dataset Information

0

3-Mercaptopyruvate sulfur transferase is a protein persulfidase


ABSTRACT: Protein S-persulfidation (P-SSH) is recognized as a common post-translational modification across all domains of life. It occurs under basal conditions and is often observed to be elevated under stress conditions. However, the mechanism(s) by which proteins are persulfidated inside cells have remained unclear. Here we report that 3-mercaptopyruvate sulfur transferase (MPST) engages in direct protein-to-protein transpersulfidation reactions beyond its previously known protein substrates thioredoxin and MOCS3/Uba4, associated with H2S generation and tRNA thiolation, respectively. We observe that depletion of MPST in human cells lowers overall intracellular protein persulfidation levels and identify a subset of proteins whose persulfidation depends on MPST. The predicted involvement of these proteins in the adaptation to stress responses supports the notion that MPST-dependent protein persulfidation promotes cytoprotective functions. The observation of MPST-independent protein persulfidation suggests that other protein persulfidases remain to be identified.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Embryonic Stem Cell

SUBMITTER: Marcin Luzarowski  

LAB HEAD: Tobias P. Dick

PROVIDER: PXD038309 | Pride | 2023-05-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
PRIDE_Sample_Description.txt Txt
Q25105-22-84-04.raw Raw
Q25105-22-84-08.raw Raw
Q25105-22-84-12.raw Raw
Q25105-22-84-16.raw Raw
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Publications

3-Mercaptopyruvate sulfur transferase is a protein persulfidase.

Pedre Brandán B   Talwar Deepti D   Barayeu Uladzimir U   Schilling Danny D   Luzarowski Marcin M   Sokolowski Mikolaj M   Glatt Sebastian S   Dick Tobias P TP  

Nature chemical biology 20230202 4


Protein S-persulfidation (P-SSH) is recognized as a common posttranslational modification. It occurs under basal conditions and is often observed to be elevated under stress conditions. However, the mechanism(s) by which proteins are persulfidated inside cells have remained unclear. Here we report that 3-mercaptopyruvate sulfur transferase (MPST) engages in direct protein-to-protein transpersulfidation reactions beyond its previously known protein substrates thioredoxin and MOCS3/Uba4, associate  ...[more]

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