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Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight

BACKGROUND: The plant-specific valine-glutamine (VQ) protein family with the conserved motif FxxxVQxLTG reportedly functions with the mitogen-activated protein kinase (MAPK) in plant immunity. However, the roles of VQ proteins in MAPK-mediated resistance to disease in rice remain largely unknown. RE...

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Autores principales: Li, Na, Yang, Zeyu, Li, Juan, Xie, Wenya, Qin, Xiaofeng, Kang, Yuanrong, Zhang, Qinglu, Li, Xianghua, Xiao, Jinghua, Ma, Haigang, Wang, Shiping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8081811/
https://www.ncbi.nlm.nih.gov/pubmed/33913048
http://dx.doi.org/10.1186/s12284-021-00483-y
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author Li, Na
Yang, Zeyu
Li, Juan
Xie, Wenya
Qin, Xiaofeng
Kang, Yuanrong
Zhang, Qinglu
Li, Xianghua
Xiao, Jinghua
Ma, Haigang
Wang, Shiping
author_facet Li, Na
Yang, Zeyu
Li, Juan
Xie, Wenya
Qin, Xiaofeng
Kang, Yuanrong
Zhang, Qinglu
Li, Xianghua
Xiao, Jinghua
Ma, Haigang
Wang, Shiping
author_sort Li, Na
collection PubMed
description BACKGROUND: The plant-specific valine-glutamine (VQ) protein family with the conserved motif FxxxVQxLTG reportedly functions with the mitogen-activated protein kinase (MAPK) in plant immunity. However, the roles of VQ proteins in MAPK-mediated resistance to disease in rice remain largely unknown. RESULTS: In this study, two rice VQ proteins OsVQ14 and OsVQ32 were newly identified to function as the signaling components of a MAPK cascade, OsMPKK6-OsMPK4, to regulate rice resistance to Xanthomonas oryzae pv. oryzae (Xoo). Both OsVQ14 and OsVQ32 positively regulated rice resistance to Xoo. In vitro and in vivo studies revealed that OsVQ14 and OsVQ32 physically interacted with and were phosphorylated by OsMPK4. OsMPK4 was highly phosphorylated in transgenic plants overexpressing OsMPKK6, which showed enhanced resistance to Xoo. Meanwhile, phosphorylated OsVQ14 and OsVQ32 were also markedly accumulated in OsMPKK6-overexpressing transgenic plants. CONCLUSIONS: We discovered that OsVQ14 and OsVQ32 functioned as substrates of the OsMPKK6-OsMPK4 cascade to enhance rice resistance to Xoo, thereby defining a more complete signal transduction pathway for induced defenses. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12284-021-00483-y.
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spelling pubmed-80818112021-05-05 Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight Li, Na Yang, Zeyu Li, Juan Xie, Wenya Qin, Xiaofeng Kang, Yuanrong Zhang, Qinglu Li, Xianghua Xiao, Jinghua Ma, Haigang Wang, Shiping Rice (N Y) Original Article BACKGROUND: The plant-specific valine-glutamine (VQ) protein family with the conserved motif FxxxVQxLTG reportedly functions with the mitogen-activated protein kinase (MAPK) in plant immunity. However, the roles of VQ proteins in MAPK-mediated resistance to disease in rice remain largely unknown. RESULTS: In this study, two rice VQ proteins OsVQ14 and OsVQ32 were newly identified to function as the signaling components of a MAPK cascade, OsMPKK6-OsMPK4, to regulate rice resistance to Xanthomonas oryzae pv. oryzae (Xoo). Both OsVQ14 and OsVQ32 positively regulated rice resistance to Xoo. In vitro and in vivo studies revealed that OsVQ14 and OsVQ32 physically interacted with and were phosphorylated by OsMPK4. OsMPK4 was highly phosphorylated in transgenic plants overexpressing OsMPKK6, which showed enhanced resistance to Xoo. Meanwhile, phosphorylated OsVQ14 and OsVQ32 were also markedly accumulated in OsMPKK6-overexpressing transgenic plants. CONCLUSIONS: We discovered that OsVQ14 and OsVQ32 functioned as substrates of the OsMPKK6-OsMPK4 cascade to enhance rice resistance to Xoo, thereby defining a more complete signal transduction pathway for induced defenses. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12284-021-00483-y. Springer US 2021-04-28 /pmc/articles/PMC8081811/ /pubmed/33913048 http://dx.doi.org/10.1186/s12284-021-00483-y Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Original Article
Li, Na
Yang, Zeyu
Li, Juan
Xie, Wenya
Qin, Xiaofeng
Kang, Yuanrong
Zhang, Qinglu
Li, Xianghua
Xiao, Jinghua
Ma, Haigang
Wang, Shiping
Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight
title Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight
title_full Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight
title_fullStr Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight
title_full_unstemmed Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight
title_short Two VQ Proteins are Substrates of the OsMPKK6-OsMPK4 Cascade in Rice Defense Against Bacterial Blight
title_sort two vq proteins are substrates of the osmpkk6-osmpk4 cascade in rice defense against bacterial blight
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8081811/
https://www.ncbi.nlm.nih.gov/pubmed/33913048
http://dx.doi.org/10.1186/s12284-021-00483-y
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