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TitleRedox-sensitive E2 Rad6 controls cellular response to oxidative stress via K63-linked ubiquitination of ribosomes.
Journal, issue, pagesCell Rep, Vol. 39, Issue 8, Page 110860, Year 2022
Publish dateMay 24, 2022
AuthorsVanessa Simões / Blanche K Cizubu / Lana Harley / Ye Zhou / Joshua Pajak / Nathan A Snyder / Jonathan Bouvette / Mario J Borgnia / Gaurav Arya / Alberto Bartesaghi / Gustavo M Silva /
PubMed AbstractProtein ubiquitination is an essential process that rapidly regulates protein synthesis, function, and fate in dynamic environments. Within its non-proteolytic functions, we showed that K63-linked ...Protein ubiquitination is an essential process that rapidly regulates protein synthesis, function, and fate in dynamic environments. Within its non-proteolytic functions, we showed that K63-linked polyubiquitinated conjugates heavily accumulate in yeast cells exposed to oxidative stress, stalling ribosomes at elongation. K63-ubiquitinated conjugates accumulate mostly because of redox inhibition of the deubiquitinating enzyme Ubp2; however, the role and regulation of ubiquitin-conjugating enzymes (E2) in this pathway remained unclear. Here, we show that the E2 Rad6 associates and modifies ribosomes during stress. We further demonstrate that Rad6 and its human homolog UBE2A are redox regulated by forming a reversible disulfide with the E1 ubiquitin-activating enzyme (Uba1). This redox regulation is part of a negative feedback regulation, which controls the levels of K63 ubiquitination under stress. Finally, we show that Rad6 activity is necessary to regulate translation, antioxidant defense, and adaptation to stress, thus providing an additional physiological role for this multifunctional enzyme.
External linksCell Rep / PubMed:35613580 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

EMDB-26440: Ribosome co-immunoprecipitation with Rad6-FLAG showing conventional 40S beak
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-26441: Ribosome co-immunoprecipitation with Rad6-FLAG showing extended conformation 40S beak
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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