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Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response
Ethylene plays its essential roles in plant development, growth, and defense responses by controlling the transcriptional reprograming, in which EIN2-C-directed regulation of histone acetylation is the first key-step for chromatin to perceive ethylene signaling. But how the nuclear acetyl coenzyme A...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10634830/ https://www.ncbi.nlm.nih.gov/pubmed/37961310 http://dx.doi.org/10.1101/2023.10.25.564010 |
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author | Shao, Zhengyao Bian, Liangqiao Ahmadi, Shyon K. Daniel, Tyler J. Belmonte, Miguel A. Burns, Jackson G. Kotla, Prashanth Bi, Yang Shen, Zhouxin Xu, Shou-Ling Wang, Zhi-Yong Briggs, Steven P. Qiao, Hong |
author_facet | Shao, Zhengyao Bian, Liangqiao Ahmadi, Shyon K. Daniel, Tyler J. Belmonte, Miguel A. Burns, Jackson G. Kotla, Prashanth Bi, Yang Shen, Zhouxin Xu, Shou-Ling Wang, Zhi-Yong Briggs, Steven P. Qiao, Hong |
author_sort | Shao, Zhengyao |
collection | PubMed |
description | Ethylene plays its essential roles in plant development, growth, and defense responses by controlling the transcriptional reprograming, in which EIN2-C-directed regulation of histone acetylation is the first key-step for chromatin to perceive ethylene signaling. But how the nuclear acetyl coenzyme A (acetyl CoA) is produced to ensure the ethylene-mediated histone acetylation is unknown. Here we report that ethylene triggers the accumulation of the pyruvate dehydrogenase complex (PDC) in the nucleus to synthesize nuclear acetyl CoA to regulate ethylene response. PDC is identified as an EIN2-C nuclear partner, and ethylene triggers its nuclear accumulation. Mutations in PDC lead to an ethylene-hyposensitivity that results from the reduction of histone acetylation and transcription activation. Enzymatically active nuclear PDC synthesize nuclear acetyl CoA for EIN2-C-directed histone acetylation and transcription regulation. These findings uncover a mechanism by which PDC-EIN2 converges the mitochondrial enzyme mediated nuclear acetyl CoA synthesis with epigenetic and transcriptional regulation for plant hormone response. |
format | Online Article Text |
id | pubmed-10634830 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-106348302023-11-13 Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response Shao, Zhengyao Bian, Liangqiao Ahmadi, Shyon K. Daniel, Tyler J. Belmonte, Miguel A. Burns, Jackson G. Kotla, Prashanth Bi, Yang Shen, Zhouxin Xu, Shou-Ling Wang, Zhi-Yong Briggs, Steven P. Qiao, Hong bioRxiv Article Ethylene plays its essential roles in plant development, growth, and defense responses by controlling the transcriptional reprograming, in which EIN2-C-directed regulation of histone acetylation is the first key-step for chromatin to perceive ethylene signaling. But how the nuclear acetyl coenzyme A (acetyl CoA) is produced to ensure the ethylene-mediated histone acetylation is unknown. Here we report that ethylene triggers the accumulation of the pyruvate dehydrogenase complex (PDC) in the nucleus to synthesize nuclear acetyl CoA to regulate ethylene response. PDC is identified as an EIN2-C nuclear partner, and ethylene triggers its nuclear accumulation. Mutations in PDC lead to an ethylene-hyposensitivity that results from the reduction of histone acetylation and transcription activation. Enzymatically active nuclear PDC synthesize nuclear acetyl CoA for EIN2-C-directed histone acetylation and transcription regulation. These findings uncover a mechanism by which PDC-EIN2 converges the mitochondrial enzyme mediated nuclear acetyl CoA synthesis with epigenetic and transcriptional regulation for plant hormone response. Cold Spring Harbor Laboratory 2023-10-27 /pmc/articles/PMC10634830/ /pubmed/37961310 http://dx.doi.org/10.1101/2023.10.25.564010 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Shao, Zhengyao Bian, Liangqiao Ahmadi, Shyon K. Daniel, Tyler J. Belmonte, Miguel A. Burns, Jackson G. Kotla, Prashanth Bi, Yang Shen, Zhouxin Xu, Shou-Ling Wang, Zhi-Yong Briggs, Steven P. Qiao, Hong Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response |
title | Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response |
title_full | Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response |
title_fullStr | Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response |
title_full_unstemmed | Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response |
title_short | Nuclear Pyruvate Dehydrogenase Complex Regulates Histone Acetylation and Transcriptional Regulation in the Ethylene Response |
title_sort | nuclear pyruvate dehydrogenase complex regulates histone acetylation and transcriptional regulation in the ethylene response |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10634830/ https://www.ncbi.nlm.nih.gov/pubmed/37961310 http://dx.doi.org/10.1101/2023.10.25.564010 |
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