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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
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.
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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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