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Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress
In plants, Vacuole H(+)‐PPases (VPPs) are important proton pumps and encoded by multiple genes. In addition to full‐length VPPs, several truncated forms are expressed, but their biological functions are unknown. In this study, we functionally characterized maize vacuole H(+)‐PPase 5 (ZmVPP5), a trun...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5071666/ https://www.ncbi.nlm.nih.gov/pubmed/26728417 http://dx.doi.org/10.1111/jipb.12462 |
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author | Sun, Xiaoliang Qi, Weiwei Yue, Yihong Ling, Huiling Wang, Gang Song, Rentao |
author_facet | Sun, Xiaoliang Qi, Weiwei Yue, Yihong Ling, Huiling Wang, Gang Song, Rentao |
author_sort | Sun, Xiaoliang |
collection | PubMed |
description | In plants, Vacuole H(+)‐PPases (VPPs) are important proton pumps and encoded by multiple genes. In addition to full‐length VPPs, several truncated forms are expressed, but their biological functions are unknown. In this study, we functionally characterized maize vacuole H(+)‐PPase 5 (ZmVPP5), a truncated VPP in the maize genome. Although ZmVPP5 shares high sequence similarity with ZmVPP1, ZmVPP5 lacks the complete structure of the conserved proton transport and the inorganic pyrophosphatase‐related domain. Phylogenetic analysis suggests that ZmVPP5 might be derived from an incomplete gene duplication event. ZmVPP5 is expressed in multiple tissues, and ZmVPP5 was detected in the plasma membrane, vacuole membrane and nuclei of maize cells. The overexpression of ZmVPP5 in yeast cells caused a hypersensitivity to salt stress. Transgenic maize lines with overexpressed ZmVPP5 also exhibited the salt hypersensitivity phenotype. A yeast two‐hybrid analysis identified the ZmBag6‐like protein as a putative ZmVPP5‐interacting protein. The results of bimolecular luminescence complementation (BiLC) assay suggest an interaction between ZmBag6‐like protein and ZmVPP5 in vivo. Overall, this study suggests that ZmVPP5 might act as a VPP antagonist and participate in the cellular response to salt stress. Our study of ZmVPP5 has expanded the understanding of the origin and functions of truncated forms of plant VPPs. |
format | Online Article Text |
id | pubmed-5071666 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-50716662016-11-02 Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress Sun, Xiaoliang Qi, Weiwei Yue, Yihong Ling, Huiling Wang, Gang Song, Rentao J Integr Plant Biol Research Articles In plants, Vacuole H(+)‐PPases (VPPs) are important proton pumps and encoded by multiple genes. In addition to full‐length VPPs, several truncated forms are expressed, but their biological functions are unknown. In this study, we functionally characterized maize vacuole H(+)‐PPase 5 (ZmVPP5), a truncated VPP in the maize genome. Although ZmVPP5 shares high sequence similarity with ZmVPP1, ZmVPP5 lacks the complete structure of the conserved proton transport and the inorganic pyrophosphatase‐related domain. Phylogenetic analysis suggests that ZmVPP5 might be derived from an incomplete gene duplication event. ZmVPP5 is expressed in multiple tissues, and ZmVPP5 was detected in the plasma membrane, vacuole membrane and nuclei of maize cells. The overexpression of ZmVPP5 in yeast cells caused a hypersensitivity to salt stress. Transgenic maize lines with overexpressed ZmVPP5 also exhibited the salt hypersensitivity phenotype. A yeast two‐hybrid analysis identified the ZmBag6‐like protein as a putative ZmVPP5‐interacting protein. The results of bimolecular luminescence complementation (BiLC) assay suggest an interaction between ZmBag6‐like protein and ZmVPP5 in vivo. Overall, this study suggests that ZmVPP5 might act as a VPP antagonist and participate in the cellular response to salt stress. Our study of ZmVPP5 has expanded the understanding of the origin and functions of truncated forms of plant VPPs. John Wiley and Sons Inc. 2016-03-27 2016-06 /pmc/articles/PMC5071666/ /pubmed/26728417 http://dx.doi.org/10.1111/jipb.12462 Text en © 2016 The Authors. Journal of Integrative Plant Biology published by John Wiley & Sons Australia, Ltd on behalf of Institute of Botany, Chinese Academy of Sciences This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs (http://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Research Articles Sun, Xiaoliang Qi, Weiwei Yue, Yihong Ling, Huiling Wang, Gang Song, Rentao Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress |
title | Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress |
title_full | Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress |
title_fullStr | Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress |
title_full_unstemmed | Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress |
title_short | Maize ZmVPP5 is a truncated Vacuole H(+)‐PPase that confers hypersensitivity to salt stress |
title_sort | maize zmvpp5 is a truncated vacuole h(+)‐ppase that confers hypersensitivity to salt stress |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5071666/ https://www.ncbi.nlm.nih.gov/pubmed/26728417 http://dx.doi.org/10.1111/jipb.12462 |
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