Cargando…

PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear

BACKGROUND: The functional characteristics of SLAC/SLAH family members isolated from Arabidopsis thaliana, poplar, barley and rice have been comprehensively investigated. However, there are no reports regarding SLAC/SLAH family genes from Rosaceae plants. RESULTS: In this study, the function of PbrS...

Descripción completa

Detalles Bibliográficos
Autores principales: Chen, Guodong, Wang, Li, Chen, Qian, Qi, Kaijie, Yin, Hao, Cao, Peng, Tang, Chao, Wu, Xiao, Zhang, Shaoling, Wang, Peng, Wu, Juyou
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6507222/
https://www.ncbi.nlm.nih.gov/pubmed/31068146
http://dx.doi.org/10.1186/s12870-019-1813-z
_version_ 1783416988161277952
author Chen, Guodong
Wang, Li
Chen, Qian
Qi, Kaijie
Yin, Hao
Cao, Peng
Tang, Chao
Wu, Xiao
Zhang, Shaoling
Wang, Peng
Wu, Juyou
author_facet Chen, Guodong
Wang, Li
Chen, Qian
Qi, Kaijie
Yin, Hao
Cao, Peng
Tang, Chao
Wu, Xiao
Zhang, Shaoling
Wang, Peng
Wu, Juyou
author_sort Chen, Guodong
collection PubMed
description BACKGROUND: The functional characteristics of SLAC/SLAH family members isolated from Arabidopsis thaliana, poplar, barley and rice have been comprehensively investigated. However, there are no reports regarding SLAC/SLAH family genes from Rosaceae plants. RESULTS: In this study, the function of PbrSLAH3, which is predominately expressed in pear (Pyrus bretschneideri) root, was investigated. PbrSLAH3 can rescue the ammonium toxicity phenomenon of slah3 mutant plants under high-ammonium/low-nitrate conditions. In addition, yeast two-hybrid and bimolecular fluorescence complementation assays confirmed that PbrSLAH3 interacts with PbrCPK32. Moreover, when PbrSLAH3 was co-expressed with either the Arabidopsis calcium-dependent protein kinase (CPK) 21 or PbrCPK32 in Xenopus oocytes, yellow fluorescence was emitted from the oocytes and typical anion currents were recorded in the presence of extracellular NO(3)(−). However, when PbrSLAH3 alone was injected, no yellow fluorescence or anion currents were recorded, suggesting that anion channel PbrSLAH3 activity was controlled through phosphorylation. Finally, electrophysiological and transgene results showed that PbrSLAH3 was more permeable to NO(3)(−) than Cl(−). CONCLUSION: We suggest that PbrSLAH3 crossing-talk with PbrCPK32 probably participate in transporting of nitrate nutrition in pear root. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12870-019-1813-z) contains supplementary material, which is available to authorized users.
format Online
Article
Text
id pubmed-6507222
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-65072222019-05-13 PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear Chen, Guodong Wang, Li Chen, Qian Qi, Kaijie Yin, Hao Cao, Peng Tang, Chao Wu, Xiao Zhang, Shaoling Wang, Peng Wu, Juyou BMC Plant Biol Research Article BACKGROUND: The functional characteristics of SLAC/SLAH family members isolated from Arabidopsis thaliana, poplar, barley and rice have been comprehensively investigated. However, there are no reports regarding SLAC/SLAH family genes from Rosaceae plants. RESULTS: In this study, the function of PbrSLAH3, which is predominately expressed in pear (Pyrus bretschneideri) root, was investigated. PbrSLAH3 can rescue the ammonium toxicity phenomenon of slah3 mutant plants under high-ammonium/low-nitrate conditions. In addition, yeast two-hybrid and bimolecular fluorescence complementation assays confirmed that PbrSLAH3 interacts with PbrCPK32. Moreover, when PbrSLAH3 was co-expressed with either the Arabidopsis calcium-dependent protein kinase (CPK) 21 or PbrCPK32 in Xenopus oocytes, yellow fluorescence was emitted from the oocytes and typical anion currents were recorded in the presence of extracellular NO(3)(−). However, when PbrSLAH3 alone was injected, no yellow fluorescence or anion currents were recorded, suggesting that anion channel PbrSLAH3 activity was controlled through phosphorylation. Finally, electrophysiological and transgene results showed that PbrSLAH3 was more permeable to NO(3)(−) than Cl(−). CONCLUSION: We suggest that PbrSLAH3 crossing-talk with PbrCPK32 probably participate in transporting of nitrate nutrition in pear root. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12870-019-1813-z) contains supplementary material, which is available to authorized users. BioMed Central 2019-05-08 /pmc/articles/PMC6507222/ /pubmed/31068146 http://dx.doi.org/10.1186/s12870-019-1813-z Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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.
spellingShingle Research Article
Chen, Guodong
Wang, Li
Chen, Qian
Qi, Kaijie
Yin, Hao
Cao, Peng
Tang, Chao
Wu, Xiao
Zhang, Shaoling
Wang, Peng
Wu, Juyou
PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
title PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
title_full PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
title_fullStr PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
title_full_unstemmed PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
title_short PbrSLAH3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
title_sort pbrslah3 is a nitrate-selective anion channel which is modulated by calcium-dependent protein kinase 32 in pear
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6507222/
https://www.ncbi.nlm.nih.gov/pubmed/31068146
http://dx.doi.org/10.1186/s12870-019-1813-z
work_keys_str_mv AT chenguodong pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT wangli pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT chenqian pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT qikaijie pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT yinhao pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT caopeng pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT tangchao pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT wuxiao pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT zhangshaoling pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT wangpeng pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear
AT wujuyou pbrslah3isanitrateselectiveanionchannelwhichismodulatedbycalciumdependentproteinkinase32inpear