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Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae
The heterotrimeric Asi ubiquitin ligase (encoded by ASI1, ASI2, and ASI3) mediates protein degradation in the inner nuclear membrane in Saccharomyces cerevisiae. Asi1p and Asi3p possess catalytic domains, while Asi2p functions as an adaptor for a subset of Asi substrates. We hypothesized the Asi com...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8170509/ https://www.ncbi.nlm.nih.gov/pubmed/34095778 http://dx.doi.org/10.17912/micropub.biology.000403 |
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author | Woodruff, Kelsey A Richards, Kyle A Evans, Melissa D Scott, Abigail R Voas, Brian M Irelan, Courtney Broshar Olesen, James B Smaldino, Philip J Rubenstein, Eric M |
author_facet | Woodruff, Kelsey A Richards, Kyle A Evans, Melissa D Scott, Abigail R Voas, Brian M Irelan, Courtney Broshar Olesen, James B Smaldino, Philip J Rubenstein, Eric M |
author_sort | Woodruff, Kelsey A |
collection | PubMed |
description | The heterotrimeric Asi ubiquitin ligase (encoded by ASI1, ASI2, and ASI3) mediates protein degradation in the inner nuclear membrane in Saccharomyces cerevisiae. Asi1p and Asi3p possess catalytic domains, while Asi2p functions as an adaptor for a subset of Asi substrates. We hypothesized the Asi complex is an important mediator of protein quality control, and we predicted that Asi would be required for optimal growth in conditions associated with elevated abundance of aberrant proteins. Loss of Asi1p or Asi3p, but not Asi2p, sensitized yeast to hygromycin B, which promotes translational infidelity by distorting the ribosome A site. Surprisingly, loss of quality control ubiquitin ligase Hul5p did not sensitize yeast to hygromycin B. Our results are consistent with a prominent role for an Asi subcomplex that includes Asi1p and Asi3p (but not Asi2p) in protein quality control. |
format | Online Article Text |
id | pubmed-8170509 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-81705092021-06-04 Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae Woodruff, Kelsey A Richards, Kyle A Evans, Melissa D Scott, Abigail R Voas, Brian M Irelan, Courtney Broshar Olesen, James B Smaldino, Philip J Rubenstein, Eric M MicroPubl Biol New Finding The heterotrimeric Asi ubiquitin ligase (encoded by ASI1, ASI2, and ASI3) mediates protein degradation in the inner nuclear membrane in Saccharomyces cerevisiae. Asi1p and Asi3p possess catalytic domains, while Asi2p functions as an adaptor for a subset of Asi substrates. We hypothesized the Asi complex is an important mediator of protein quality control, and we predicted that Asi would be required for optimal growth in conditions associated with elevated abundance of aberrant proteins. Loss of Asi1p or Asi3p, but not Asi2p, sensitized yeast to hygromycin B, which promotes translational infidelity by distorting the ribosome A site. Surprisingly, loss of quality control ubiquitin ligase Hul5p did not sensitize yeast to hygromycin B. Our results are consistent with a prominent role for an Asi subcomplex that includes Asi1p and Asi3p (but not Asi2p) in protein quality control. Caltech Library 2021-06-01 /pmc/articles/PMC8170509/ /pubmed/34095778 http://dx.doi.org/10.17912/micropub.biology.000403 Text en Copyright: © 2021 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Woodruff, Kelsey A Richards, Kyle A Evans, Melissa D Scott, Abigail R Voas, Brian M Irelan, Courtney Broshar Olesen, James B Smaldino, Philip J Rubenstein, Eric M Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae |
title | Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae |
title_full | Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae |
title_fullStr | Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae |
title_full_unstemmed | Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae |
title_short | Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae |
title_sort | inner nuclear membrane asi ubiquitin ligase catalytic subunits asi1p and asi3p, but not asi2p, confer resistance to aminoglycoside hygromycin b in saccharomyces cerevisiae |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8170509/ https://www.ncbi.nlm.nih.gov/pubmed/34095778 http://dx.doi.org/10.17912/micropub.biology.000403 |
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