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DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis
Maintaining mitochondrial proteome integrity is especially important under stress conditions to ensure a continued ATP supply for protection and adaptation responses in plants. Deg/HtrA proteases are important factors in the cellular protein quality control system, but little is known about their fu...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793672/ https://www.ncbi.nlm.nih.gov/pubmed/31225599 http://dx.doi.org/10.1093/jxb/erz294 |
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author | Huber, Catharina V Jakobs, Barbara D Mishra, Laxmi S Niedermaier, Stefan Stift, Marc Winter, Gudrun Adamska, Iwona Funk, Christiane Huesgen, Pitter F Funck, Dietmar |
author_facet | Huber, Catharina V Jakobs, Barbara D Mishra, Laxmi S Niedermaier, Stefan Stift, Marc Winter, Gudrun Adamska, Iwona Funk, Christiane Huesgen, Pitter F Funck, Dietmar |
author_sort | Huber, Catharina V |
collection | PubMed |
description | Maintaining mitochondrial proteome integrity is especially important under stress conditions to ensure a continued ATP supply for protection and adaptation responses in plants. Deg/HtrA proteases are important factors in the cellular protein quality control system, but little is known about their function in mitochondria. Here we analyzed the expression pattern and physiological function of Arabidopsis thaliana DEG10, which has homologs in all photosynthetic eukaryotes. Both expression of DEG10:GFP fusion proteins and immunoblotting after cell fractionation showed an unambiguous subcellular localization exclusively in mitochondria. DEG10 promoter:GUS fusion constructs showed that DEG10 is expressed in trichomes but also in the vascular tissue of roots and aboveground organs. DEG10 loss-of-function mutants were impaired in root elongation, especially at elevated temperature. Quantitative proteome analysis revealed concomitant changes in the abundance of mitochondrial respiratory chain components and assembly factors, which partially appeared to depend on altered mitochondrial retrograde signaling. Under field conditions, lack of DEG10 caused a decrease in seed production. Taken together, our findings demonstrate that DEG10 affects mitochondrial proteostasis, is required for optimal root development and seed set under challenging environmental conditions, and thus contributes to stress tolerance of plants. |
format | Online Article Text |
id | pubmed-6793672 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-67936722019-10-18 DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis Huber, Catharina V Jakobs, Barbara D Mishra, Laxmi S Niedermaier, Stefan Stift, Marc Winter, Gudrun Adamska, Iwona Funk, Christiane Huesgen, Pitter F Funck, Dietmar J Exp Bot Research Papers Maintaining mitochondrial proteome integrity is especially important under stress conditions to ensure a continued ATP supply for protection and adaptation responses in plants. Deg/HtrA proteases are important factors in the cellular protein quality control system, but little is known about their function in mitochondria. Here we analyzed the expression pattern and physiological function of Arabidopsis thaliana DEG10, which has homologs in all photosynthetic eukaryotes. Both expression of DEG10:GFP fusion proteins and immunoblotting after cell fractionation showed an unambiguous subcellular localization exclusively in mitochondria. DEG10 promoter:GUS fusion constructs showed that DEG10 is expressed in trichomes but also in the vascular tissue of roots and aboveground organs. DEG10 loss-of-function mutants were impaired in root elongation, especially at elevated temperature. Quantitative proteome analysis revealed concomitant changes in the abundance of mitochondrial respiratory chain components and assembly factors, which partially appeared to depend on altered mitochondrial retrograde signaling. Under field conditions, lack of DEG10 caused a decrease in seed production. Taken together, our findings demonstrate that DEG10 affects mitochondrial proteostasis, is required for optimal root development and seed set under challenging environmental conditions, and thus contributes to stress tolerance of plants. Oxford University Press 2019-10-01 2019-06-20 /pmc/articles/PMC6793672/ /pubmed/31225599 http://dx.doi.org/10.1093/jxb/erz294 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Papers Huber, Catharina V Jakobs, Barbara D Mishra, Laxmi S Niedermaier, Stefan Stift, Marc Winter, Gudrun Adamska, Iwona Funk, Christiane Huesgen, Pitter F Funck, Dietmar DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis |
title | DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis |
title_full | DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis |
title_fullStr | DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis |
title_full_unstemmed | DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis |
title_short | DEG10 contributes to mitochondrial proteostasis, root growth, and seed yield in Arabidopsis |
title_sort | deg10 contributes to mitochondrial proteostasis, root growth, and seed yield in arabidopsis |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793672/ https://www.ncbi.nlm.nih.gov/pubmed/31225599 http://dx.doi.org/10.1093/jxb/erz294 |
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