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Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing
The phytohormone abscisic acid (ABA) plays pivotal roles in the regulation of developmental and environmental responses in plants. Identification of cytoplasmic ABA receptors enabled the elucidation of the main ABA signalling pathway, connecting ABA perception to either nuclear events or the action...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3430999/ https://www.ncbi.nlm.nih.gov/pubmed/22821940 http://dx.doi.org/10.1093/jxb/ers188 |
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author | Murayama, Maki Hayashi, Shimpei Nishimura, Noriyuki Ishide, Mayumi Kobayashi, Keiko Yagi, Yusuke Asami, Tadao Nakamura, Takahiro Shinozaki, Kazuo Hirayama, Takashi |
author_facet | Murayama, Maki Hayashi, Shimpei Nishimura, Noriyuki Ishide, Mayumi Kobayashi, Keiko Yagi, Yusuke Asami, Tadao Nakamura, Takahiro Shinozaki, Kazuo Hirayama, Takashi |
author_sort | Murayama, Maki |
collection | PubMed |
description | The phytohormone abscisic acid (ABA) plays pivotal roles in the regulation of developmental and environmental responses in plants. Identification of cytoplasmic ABA receptors enabled the elucidation of the main ABA signalling pathway, connecting ABA perception to either nuclear events or the action of several transporters. However, the physiological functions of ABA in cellular processes largely remain unknown. To obtain greater insight into the ABA response, genetic screening was performed to isolate ABA-related mutants of Arabidopsis and several novel ABA-hypersensitive mutants were isolated. One of those mutants—ahg11—was characterized further. Map-based cloning showed that AHG11 encodes a PPR type protein, which has potential roles in RNA editing. An AHG11-GFP fusion protein indicated that AHG11 mainly localized to the mitochondria. Consistent with this observation, the nad4 transcript, which normally undergoes RNA editing, lacks a single RNA editing event conferring a conversion of an amino acid residue in ahg11 mutants. The geminating ahg11 seeds have higher levels of reactive-oxygen-species-responsive genes. Presumably, partial impairment of mitochondrial function caused by an amino acid conversion in one of the complex I components induces redox imbalance which, in turn, confers an abnormal response to the plant hormone. |
format | Online Article Text |
id | pubmed-3430999 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-34309992012-08-30 Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing Murayama, Maki Hayashi, Shimpei Nishimura, Noriyuki Ishide, Mayumi Kobayashi, Keiko Yagi,
Yusuke Asami, Tadao Nakamura, Takahiro Shinozaki, Kazuo Hirayama, Takashi J Exp Bot Research Paper The phytohormone abscisic acid (ABA) plays pivotal roles in the regulation of developmental and environmental responses in plants. Identification of cytoplasmic ABA receptors enabled the elucidation of the main ABA signalling pathway, connecting ABA perception to either nuclear events or the action of several transporters. However, the physiological functions of ABA in cellular processes largely remain unknown. To obtain greater insight into the ABA response, genetic screening was performed to isolate ABA-related mutants of Arabidopsis and several novel ABA-hypersensitive mutants were isolated. One of those mutants—ahg11—was characterized further. Map-based cloning showed that AHG11 encodes a PPR type protein, which has potential roles in RNA editing. An AHG11-GFP fusion protein indicated that AHG11 mainly localized to the mitochondria. Consistent with this observation, the nad4 transcript, which normally undergoes RNA editing, lacks a single RNA editing event conferring a conversion of an amino acid residue in ahg11 mutants. The geminating ahg11 seeds have higher levels of reactive-oxygen-species-responsive genes. Presumably, partial impairment of mitochondrial function caused by an amino acid conversion in one of the complex I components induces redox imbalance which, in turn, confers an abnormal response to the plant hormone. Oxford University Press 2012-09 2012-08-29 /pmc/articles/PMC3430999/ /pubmed/22821940 http://dx.doi.org/10.1093/jxb/ers188 Text en © The Author [2012]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0/uk/) which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Murayama, Maki Hayashi, Shimpei Nishimura, Noriyuki Ishide, Mayumi Kobayashi, Keiko Yagi, Yusuke Asami, Tadao Nakamura, Takahiro Shinozaki, Kazuo Hirayama, Takashi Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing |
title | Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing |
title_full | Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing |
title_fullStr | Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing |
title_full_unstemmed | Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing |
title_short | Isolation of Arabidopsis ahg11, a weak ABA hypersensitive mutant defective in nad4 RNA editing |
title_sort | isolation of arabidopsis ahg11, a weak aba hypersensitive mutant defective in nad4 rna editing |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3430999/ https://www.ncbi.nlm.nih.gov/pubmed/22821940 http://dx.doi.org/10.1093/jxb/ers188 |
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