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Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance

BACKGROUND: Rice is a chilling-sensitive crop that would suffer serious damage from low temperatures. Overexpression of the Lsi1 gene (Lsi1-OX) in rice enhances its chilling tolerance. This study revealed that a serine hydroxymethyltransferase (OsSHMT) mainly localised in the endoplasmic reticulum (...

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Autores principales: Fang, Changxun, Zhang, Pengli, Li, Lanlan, Yang, Luke, Mu, Dan, Yan, Xue, Li, Zhong, Lin, Wenxiong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7249644/
https://www.ncbi.nlm.nih.gov/pubmed/32456700
http://dx.doi.org/10.1186/s12870-020-02446-9
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author Fang, Changxun
Zhang, Pengli
Li, Lanlan
Yang, Luke
Mu, Dan
Yan, Xue
Li, Zhong
Lin, Wenxiong
author_facet Fang, Changxun
Zhang, Pengli
Li, Lanlan
Yang, Luke
Mu, Dan
Yan, Xue
Li, Zhong
Lin, Wenxiong
author_sort Fang, Changxun
collection PubMed
description BACKGROUND: Rice is a chilling-sensitive crop that would suffer serious damage from low temperatures. Overexpression of the Lsi1 gene (Lsi1-OX) in rice enhances its chilling tolerance. This study revealed that a serine hydroxymethyltransferase (OsSHMT) mainly localised in the endoplasmic reticulum (ER) is involved in increasing tolerance to chilling. RESULTS: A higher transcription level of OsSHMT was detected in Lsi1-OX rice than in the wild type. Histone H1 and nucleic acid binding protein were found to bind to the promoter region of OsSHMT and regulate its expression, and the transcription levels of these proteins were also up-regulated in the Lsi1-OX rice. Moreover, OsSHMT interacts with ATP synthase subunit α, heat shock protein Hsp70, mitochondrial substrate carrier family protein, ascorbate peroxidase 1 and ATP synthase subunit β. Lsi1-encoded protein OsNIP2;1 also interacts with ATP synthase subunit β, and the coordination of these proteins appears to function in reducing reactive oxygen species, as the H(2)O(2) content of transgenic OsSHMT Arabidopsis thaliana was lower than that of the non-transgenic line under chilling treatment. CONCLUSIONS: Our results indicate that ER-localised OsSHMT plays a role in scavenging H(2)O(2) to enhance the chilling tolerance of Lsi1-OX rice and that ATP synthase subunit β is an intermediate junction between OsNIP2;1 and OsSHMT.
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spelling pubmed-72496442020-06-04 Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance Fang, Changxun Zhang, Pengli Li, Lanlan Yang, Luke Mu, Dan Yan, Xue Li, Zhong Lin, Wenxiong BMC Plant Biol Research Article BACKGROUND: Rice is a chilling-sensitive crop that would suffer serious damage from low temperatures. Overexpression of the Lsi1 gene (Lsi1-OX) in rice enhances its chilling tolerance. This study revealed that a serine hydroxymethyltransferase (OsSHMT) mainly localised in the endoplasmic reticulum (ER) is involved in increasing tolerance to chilling. RESULTS: A higher transcription level of OsSHMT was detected in Lsi1-OX rice than in the wild type. Histone H1 and nucleic acid binding protein were found to bind to the promoter region of OsSHMT and regulate its expression, and the transcription levels of these proteins were also up-regulated in the Lsi1-OX rice. Moreover, OsSHMT interacts with ATP synthase subunit α, heat shock protein Hsp70, mitochondrial substrate carrier family protein, ascorbate peroxidase 1 and ATP synthase subunit β. Lsi1-encoded protein OsNIP2;1 also interacts with ATP synthase subunit β, and the coordination of these proteins appears to function in reducing reactive oxygen species, as the H(2)O(2) content of transgenic OsSHMT Arabidopsis thaliana was lower than that of the non-transgenic line under chilling treatment. CONCLUSIONS: Our results indicate that ER-localised OsSHMT plays a role in scavenging H(2)O(2) to enhance the chilling tolerance of Lsi1-OX rice and that ATP synthase subunit β is an intermediate junction between OsNIP2;1 and OsSHMT. BioMed Central 2020-05-26 /pmc/articles/PMC7249644/ /pubmed/32456700 http://dx.doi.org/10.1186/s12870-020-02446-9 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research Article
Fang, Changxun
Zhang, Pengli
Li, Lanlan
Yang, Luke
Mu, Dan
Yan, Xue
Li, Zhong
Lin, Wenxiong
Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance
title Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance
title_full Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance
title_fullStr Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance
title_full_unstemmed Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance
title_short Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H(2)O(2) to enhance rice chilling tolerance
title_sort serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging h(2)o(2) to enhance rice chilling tolerance
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7249644/
https://www.ncbi.nlm.nih.gov/pubmed/32456700
http://dx.doi.org/10.1186/s12870-020-02446-9
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