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The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence
The 26S proteasome is a conserved multi-subunit machinery in eukaryotes. It selectively degrades ubiquitinated proteins, which in turn provides an efficient molecular mechanism to regulate numerous cellular functions and developmental processes. Here, we studied a new loss-of-function allele of RPN1...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9525688/ https://www.ncbi.nlm.nih.gov/pubmed/36180574 http://dx.doi.org/10.1038/s42003-022-03998-2 |
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author | Boussardon, Clément Bag, Pushan Juvany, Marta Šimura, Jan Ljung, Karin Jansson, Stefan Keech, Olivier |
author_facet | Boussardon, Clément Bag, Pushan Juvany, Marta Šimura, Jan Ljung, Karin Jansson, Stefan Keech, Olivier |
author_sort | Boussardon, Clément |
collection | PubMed |
description | The 26S proteasome is a conserved multi-subunit machinery in eukaryotes. It selectively degrades ubiquitinated proteins, which in turn provides an efficient molecular mechanism to regulate numerous cellular functions and developmental processes. Here, we studied a new loss-of-function allele of RPN12a, a plant ortholog of the yeast and human structural component of the 19S proteasome RPN12. Combining a set of biochemical and molecular approaches, we confirmed that a rpn12a knock-out had exacerbated 20S and impaired 26S activities. The altered proteasomal activity led to a pleiotropic phenotype affecting both the vegetative growth and reproductive phase of the plant, including a striking repression of leaf senescence associate cell-death. Further investigation demonstrated that RPN12a is involved in the regulation of several conjugates associated with the auxin, cytokinin, ethylene and jasmonic acid homeostasis. Such enhanced aptitude of plant cells for survival in rpn12a contrasts with reports on animals, where 26S proteasome mutants generally show an accelerated cell death phenotype. |
format | Online Article Text |
id | pubmed-9525688 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-95256882022-10-02 The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence Boussardon, Clément Bag, Pushan Juvany, Marta Šimura, Jan Ljung, Karin Jansson, Stefan Keech, Olivier Commun Biol Article The 26S proteasome is a conserved multi-subunit machinery in eukaryotes. It selectively degrades ubiquitinated proteins, which in turn provides an efficient molecular mechanism to regulate numerous cellular functions and developmental processes. Here, we studied a new loss-of-function allele of RPN12a, a plant ortholog of the yeast and human structural component of the 19S proteasome RPN12. Combining a set of biochemical and molecular approaches, we confirmed that a rpn12a knock-out had exacerbated 20S and impaired 26S activities. The altered proteasomal activity led to a pleiotropic phenotype affecting both the vegetative growth and reproductive phase of the plant, including a striking repression of leaf senescence associate cell-death. Further investigation demonstrated that RPN12a is involved in the regulation of several conjugates associated with the auxin, cytokinin, ethylene and jasmonic acid homeostasis. Such enhanced aptitude of plant cells for survival in rpn12a contrasts with reports on animals, where 26S proteasome mutants generally show an accelerated cell death phenotype. Nature Publishing Group UK 2022-09-30 /pmc/articles/PMC9525688/ /pubmed/36180574 http://dx.doi.org/10.1038/s42003-022-03998-2 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Boussardon, Clément Bag, Pushan Juvany, Marta Šimura, Jan Ljung, Karin Jansson, Stefan Keech, Olivier The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
title | The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
title_full | The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
title_fullStr | The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
title_full_unstemmed | The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
title_short | The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
title_sort | rpn12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9525688/ https://www.ncbi.nlm.nih.gov/pubmed/36180574 http://dx.doi.org/10.1038/s42003-022-03998-2 |
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