AI Article Synopsis

  • The study investigates how hydrogen peroxide (HO) affects protein function by reversible oxidation of thiols, emphasizing its role in cellular signaling.
  • Researchers created a yeast library with a HO sensor (HyPer7) attached to proteins to identify locations of HO generation, alongside a control library with a mutant sensor.
  • Results showed that HO availability varies significantly among different proteins and conditions, indicating that HO generation is more localized and nuanced than previously thought.

Article Abstract

Hydrogen peroxide (HO) sensing and signaling involves the reversible oxidation of particular thiols on particular proteins to modulate protein function in a dynamic manner. HO can be generated from various intracellular sources, but their identities and relative contributions are often unknown. To identify endogenous "hotspots" of HO generation on the scale of individual proteins and protein complexes, we generated a yeast library in which the HO 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 HO-generating environments. Screening under a variety of different metabolic conditions revealed dynamic changes in HO availability highly specific to individual proteins and protein complexes. These findings suggest that intracellular HO generation is much more localized and functionally differentiated than previously recognized.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10691247PMC
http://dx.doi.org/10.1073/pnas.2314043120DOI Listing

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