TY  - JOUR
AU  - Kritsiligkou, Paraskevi
AU  - Bosch, Katharina
AU  - Shen, Tzu-Keng
AU  - Meurer, Matthias
AU  - Knop, Michael
AU  - Dick, Tobias
TI  - Proteome-wide tagging with an H2O2 biosensor reveals highly localized and dynamic redox microenvironments.
JO  - Proceedings of the National Academy of Sciences of the United States of America
VL  - 120
IS  - 48
SN  - 0027-8424
CY  - Washington, DC
PB  - National Acad. of Sciences
M1  - DKFZ-2023-02434
SP  - e2314043120
PY  - 2023
N1  - DKFZ-ZMBH Alliance  / #EA:A160#LA:A160# / 2023 Nov 28;120(48):e2314043120
AB  - Hydrogen peroxide (H2O2) sensing and signaling involves the reversible oxidation of particular thiols on particular proteins to modulate protein function in a dynamic manner. H2O2 can be generated from various intracellular sources, but their identities and relative contributions are often unknown. To identify endogenous 'hotspots' of H2O2 generation on the scale of individual proteins and protein complexes, we generated a yeast library in which the H2O2 sensor HyPer7 was fused to the C-terminus of all protein-coding open reading frames (ORFs). We also generated a control library in which a redox-insensitive mutant of HyPer7 (SypHer7) was fused to all ORFs. Both libraries were screened side-by-side to identify proteins located within H2O2-generating environments. Screening under a variety of different metabolic conditions revealed dynamic changes in H2O2 availability highly specific to individual proteins and protein complexes. These findings suggest that intracellular H2O2 generation is much more localized and functionally differentiated than previously recognized.
KW  - genetically encoded probes (Other)
KW  - hydrogen peroxide (Other)
KW  - redox regulation (Other)
KW  - redox signaling (Other)
LB  - PUB:(DE-HGF)16
C6  - pmid:37991942
DO  - DOI:10.1073/pnas.2314043120
UR  - https://inrepo02.dkfz.de/record/285568
ER  -