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HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes
Histone deacetylases (HDAs) play an important role in transcriptional regulation of multiple biological processes. In this study, we investigated the function of HDA15 in abscisic acid (ABA) responses. We used immunopurification coupled with mass spectrometry-based proteomics to identify proteins in...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9434327/ https://www.ncbi.nlm.nih.gov/pubmed/35670741 http://dx.doi.org/10.1093/plphys/kiac271 |
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author | Tu, Yi-Tsung Chen, Chia-Yang Huang, Yi-Sui Chang, Chung-Han Yen, Ming-Ren Hsieh, Jo-Wei Allison Chen, Pao-Yang Wu, Keqiang |
author_facet | Tu, Yi-Tsung Chen, Chia-Yang Huang, Yi-Sui Chang, Chung-Han Yen, Ming-Ren Hsieh, Jo-Wei Allison Chen, Pao-Yang Wu, Keqiang |
author_sort | Tu, Yi-Tsung |
collection | PubMed |
description | Histone deacetylases (HDAs) play an important role in transcriptional regulation of multiple biological processes. In this study, we investigated the function of HDA15 in abscisic acid (ABA) responses. We used immunopurification coupled with mass spectrometry-based proteomics to identify proteins interacting with HDA15 in Arabidopsis (Arabidopsis thaliana). HDA15 interacted with the core subunits of the MOS4-associated complex (MAC), MAC3A and MAC3B, with interaction between HDA15 and MAC3B enhanced by ABA. hda15 and mac3a/mac3b mutants were ABA-insensitive during seed germination and hyposensitive to salinity. RNA sequencing analysis demonstrated that HDA15 and MAC3A/MAC3B co-regulate ABA-responsive intron retention (IR). Furthermore, HDA15 reduced the histone acetylation level of genomic regions near ABA-responsive IR sites and the association of MAC3B with ABA-responsive pre-mRNA was dependent on HDA15. Our results indicate that HDA15 is involved in ABA responses by interacting with MAC3A/MAC3B to mediate splicing of introns. |
format | Online Article Text |
id | pubmed-9434327 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-94343272022-09-01 HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes Tu, Yi-Tsung Chen, Chia-Yang Huang, Yi-Sui Chang, Chung-Han Yen, Ming-Ren Hsieh, Jo-Wei Allison Chen, Pao-Yang Wu, Keqiang Plant Physiol Focus Issue on Evolution of Plant Structure and Function Histone deacetylases (HDAs) play an important role in transcriptional regulation of multiple biological processes. In this study, we investigated the function of HDA15 in abscisic acid (ABA) responses. We used immunopurification coupled with mass spectrometry-based proteomics to identify proteins interacting with HDA15 in Arabidopsis (Arabidopsis thaliana). HDA15 interacted with the core subunits of the MOS4-associated complex (MAC), MAC3A and MAC3B, with interaction between HDA15 and MAC3B enhanced by ABA. hda15 and mac3a/mac3b mutants were ABA-insensitive during seed germination and hyposensitive to salinity. RNA sequencing analysis demonstrated that HDA15 and MAC3A/MAC3B co-regulate ABA-responsive intron retention (IR). Furthermore, HDA15 reduced the histone acetylation level of genomic regions near ABA-responsive IR sites and the association of MAC3B with ABA-responsive pre-mRNA was dependent on HDA15. Our results indicate that HDA15 is involved in ABA responses by interacting with MAC3A/MAC3B to mediate splicing of introns. Oxford University Press 2022-06-07 /pmc/articles/PMC9434327/ /pubmed/35670741 http://dx.doi.org/10.1093/plphys/kiac271 Text en © The Author(s) 2022. 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 (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 | Focus Issue on Evolution of Plant Structure and Function Tu, Yi-Tsung Chen, Chia-Yang Huang, Yi-Sui Chang, Chung-Han Yen, Ming-Ren Hsieh, Jo-Wei Allison Chen, Pao-Yang Wu, Keqiang HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes |
title | HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes |
title_full | HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes |
title_fullStr | HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes |
title_full_unstemmed | HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes |
title_short | HISTONE DEACETYLASE 15 and MOS4-associated complex subunits 3A/3B coregulate intron retention of ABA-responsive genes |
title_sort | histone deacetylase 15 and mos4-associated complex subunits 3a/3b coregulate intron retention of aba-responsive genes |
topic | Focus Issue on Evolution of Plant Structure and Function |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9434327/ https://www.ncbi.nlm.nih.gov/pubmed/35670741 http://dx.doi.org/10.1093/plphys/kiac271 |
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