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

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 confer resistance to hygromycin B, whic...

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Bibliographic Details
Published in:	microPublication biology Vol. 2024
Main Authors:	Owutey, Sophia L, Procuniar, Katrina A, Akoto, Emmanuel, Davis, Jacob C, Vachon, Rachel M, O'Malley, LiLi F, Schneider, Hayden O, Smaldino, Philip J, True, Jason D, Kalinski, Ashley L, Rubenstein, Eric M
Format:	Journal Article
Language:	English
Published:	United States Caltech Library 2024
Subjects:	New Finding Phenotype Data S. Cerevisiae
Online Access:	Get full text
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Summary:	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 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 deletion having a greater impact, consistent with characterized roles for Ubc6 and Ubc7 in ER and INM protein quality control.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 The authors declare that there are no conflicts of interest present.
ISSN:	2578-9430 2578-9430
DOI:	10.17912/micropub.biology.001276