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000285568 1001_ $$0P:(DE-He78)57343d900abd5ee285eb0533cb29208d$$aKritsiligkou, Paraskevi$$b0$$eFirst author$$udkfz
000285568 245__ $$aProteome-wide tagging with an H2O2 biosensor reveals highly localized and dynamic redox microenvironments.
000285568 260__ $$aWashington, DC$$bNational Acad. of Sciences$$c2023
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000285568 520__ $$aHydrogen 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.
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000285568 650_7 $$2Other$$agenetically encoded probes
000285568 650_7 $$2Other$$ahydrogen peroxide
000285568 650_7 $$2Other$$aredox regulation
000285568 650_7 $$2Other$$aredox signaling
000285568 7001_ $$0P:(DE-He78)06726f839165763c31adcbf12daf3316$$aBosch, Katharina$$b1$$eFirst author$$udkfz
000285568 7001_ $$0P:(DE-He78)9aff7e97895c11ff30a2425dea169cb9$$aShen, Tzu-Keng$$b2
000285568 7001_ $$0P:(DE-He78)1dcea7102ac9356741b71995e7460c46$$aMeurer, Matthias$$b3
000285568 7001_ $$0P:(DE-He78)03ae15a30a7fa7191475148bf4e7f581$$aKnop, Michael$$b4$$udkfz
000285568 7001_ $$0P:(DE-He78)7f55a0ed8b021080de00960cc73768fb$$aDick, Tobias$$b5$$eLast author$$udkfz
000285568 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.2314043120$$gVol. 120, no. 48, p. e2314043120$$n48$$pe2314043120$$tProceedings of the National Academy of Sciences of the United States of America$$v120$$x0027-8424$$y2023
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