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mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth
The quality control system for messenger RNA (mRNA) is fundamental for cellular activities in eukaryotes. To elucidate the molecular mechanism of 3′-phosphoinositide-dependent protein kinase1 (PDK1), a master regulator that is essential throughout eukaryotic growth and development, we employed a for...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8331137/ https://www.ncbi.nlm.nih.gov/pubmed/33930167 http://dx.doi.org/10.1093/plphys/kiab199 |
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author | Kong, Wei Tan, Shutang Zhao, Qing Lin, De-Li Xu, Zhi-Hong Friml, Jiří Xue, Hong-Wei |
author_facet | Kong, Wei Tan, Shutang Zhao, Qing Lin, De-Li Xu, Zhi-Hong Friml, Jiří Xue, Hong-Wei |
author_sort | Kong, Wei |
collection | PubMed |
description | The quality control system for messenger RNA (mRNA) is fundamental for cellular activities in eukaryotes. To elucidate the molecular mechanism of 3′-phosphoinositide-dependent protein kinase1 (PDK1), a master regulator that is essential throughout eukaryotic growth and development, we employed a forward genetic approach to screen for suppressors of the loss-of-function T-DNA insertion double mutant pdk1.1 pdk1.2 in Arabidopsis thaliana. Notably, the severe growth attenuation of pdk1.1 pdk1.2 was rescued by sop21 (suppressor of pdk1.1 pdk1.2), which harbors a loss-of-function mutation in PELOTA1 (PEL1). PEL1 is a homolog of mammalian PELOTA and yeast (Saccharomyces cerevisiae) DOM34p, which each form a heterodimeric complex with the GTPase HBS1 (HSP70 SUBFAMILY B SUPPRESSOR1, also called SUPERKILLER PROTEIN7, SKI7), a protein that is responsible for ribosomal rescue and thereby assures the quality and fidelity of mRNA molecules during translation. Genetic analysis further revealed that a dysfunctional PEL1–HBS1 complex failed to degrade the T-DNA-disrupted PDK1 transcripts, which were truncated but functional, and thus rescued the growth and developmental defects of pdk1.1 pdk1.2. Our studies demonstrated the functionality of a homologous PELOTA–HBS1 complex and identified its essential regulatory role in plants, providing insights into the mechanism of mRNA quality control. |
format | Online Article Text |
id | pubmed-8331137 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-83311372021-08-04 mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth Kong, Wei Tan, Shutang Zhao, Qing Lin, De-Li Xu, Zhi-Hong Friml, Jiří Xue, Hong-Wei Plant Physiol Research Articles The quality control system for messenger RNA (mRNA) is fundamental for cellular activities in eukaryotes. To elucidate the molecular mechanism of 3′-phosphoinositide-dependent protein kinase1 (PDK1), a master regulator that is essential throughout eukaryotic growth and development, we employed a forward genetic approach to screen for suppressors of the loss-of-function T-DNA insertion double mutant pdk1.1 pdk1.2 in Arabidopsis thaliana. Notably, the severe growth attenuation of pdk1.1 pdk1.2 was rescued by sop21 (suppressor of pdk1.1 pdk1.2), which harbors a loss-of-function mutation in PELOTA1 (PEL1). PEL1 is a homolog of mammalian PELOTA and yeast (Saccharomyces cerevisiae) DOM34p, which each form a heterodimeric complex with the GTPase HBS1 (HSP70 SUBFAMILY B SUPPRESSOR1, also called SUPERKILLER PROTEIN7, SKI7), a protein that is responsible for ribosomal rescue and thereby assures the quality and fidelity of mRNA molecules during translation. Genetic analysis further revealed that a dysfunctional PEL1–HBS1 complex failed to degrade the T-DNA-disrupted PDK1 transcripts, which were truncated but functional, and thus rescued the growth and developmental defects of pdk1.1 pdk1.2. Our studies demonstrated the functionality of a homologous PELOTA–HBS1 complex and identified its essential regulatory role in plants, providing insights into the mechanism of mRNA quality control. Oxford University Press 2021-04-30 /pmc/articles/PMC8331137/ /pubmed/33930167 http://dx.doi.org/10.1093/plphys/kiab199 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Articles Kong, Wei Tan, Shutang Zhao, Qing Lin, De-Li Xu, Zhi-Hong Friml, Jiří Xue, Hong-Wei mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
title | mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
title_full | mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
title_fullStr | mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
title_full_unstemmed | mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
title_short | mRNA surveillance complex PELOTA–HBS1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
title_sort | mrna surveillance complex pelota–hbs1 regulates phosphoinositide-dependent protein kinase1 and plant growth |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8331137/ https://www.ncbi.nlm.nih.gov/pubmed/33930167 http://dx.doi.org/10.1093/plphys/kiab199 |
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