Endoplasmic reticulum and inner nuclear membrane ubiquitin-conjugating enzymes Ubc6 and Ubc7 confer resistance to hygromycin B in Saccharomyces cerevisiae .

Autor: Owutey SL; Department of Biology, Ball State University., Procuniar KA; Department of Biology, Ball State University., Akoto E; Department of Biology, Ball State University., Davis JC; Department of Biology, Ball State University.; Department of Anesthesiology, University of North Carolina., Vachon RM; Department of Biology, Ball State University., O'Malley LF; Department of Biology, Ball State University., Schneider HO; Department of Biology, Ball State University.; Division of Molecular Cardiovascular Biology, Cincinnati Children's Hospital Medical Center., Smaldino PJ; Department of Biology, Ball State University., True JD; Department of Biology, Ball State University., Kalinski AL; Department of Biology, Ball State University., Rubenstein EM; Department of Biology, Ball State University.
Jazyk: angličtina
Zdroj: MicroPublication biology [MicroPubl Biol] 2024 Jul 29; Vol. 2024. Date of Electronic Publication: 2024 Jul 29 (Print Publication: 2024).
DOI: 10.17912/micropub.biology.001276
Abstrakt: Aberrant endoplasmic reticulum (ER) and inner nuclear membrane (INM) proteins are destroyed through ER-associated degradation (ERAD) and INM-associated degradation (INMAD). We previously showed the Hrd1, Doa10, and Asi ERAD and INMAD ubiquitin ligases (E3s) in Saccharomyces cerevisiae confer resistance to hygromycin B, which distorts the ribosome decoding center. Here, we assessed the requirement of Ubc6 and Ubc7, the primary ERAD and INMAD ubiquitin-conjugating enzymes (E2s) for hygromycin B resistance. Loss of either E2 sensitized cells to hygromycin B, with UBC7 deletion having a greater impact, consistent with characterized roles for Ubc6 and Ubc7 in ER and INM protein quality control.
Competing Interests: The authors declare that there are no conflicts of interest present.
(Copyright: © 2024 by the authors.)
Databáze: MEDLINE
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