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An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana
Aquaporins (AQPs) are essential channel proteins that play central roles in maintaining water homeostasis. Here, a novel aquaporin gene, named KoPIP2;1, was cloned from the mangrove plant Kandelia obovata by RACE technology. The KoPIP2;1 gene was 1404 bp in length with an open reading frame (ORF) of...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10376877/ https://www.ncbi.nlm.nih.gov/pubmed/37508905 http://dx.doi.org/10.3390/bioengineering10070878 |
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author | Fei, Jiao Wang, Youshao Cheng, Hao Wang, Hui Wu, Meilin Sun, Fulin Sun, Cuici |
author_facet | Fei, Jiao Wang, Youshao Cheng, Hao Wang, Hui Wu, Meilin Sun, Fulin Sun, Cuici |
author_sort | Fei, Jiao |
collection | PubMed |
description | Aquaporins (AQPs) are essential channel proteins that play central roles in maintaining water homeostasis. Here, a novel aquaporin gene, named KoPIP2;1, was cloned from the mangrove plant Kandelia obovata by RACE technology. The KoPIP2;1 gene was 1404 bp in length with an open reading frame (ORF) of 852 bp, encoded with 283 amino acids. Database comparisons revealed that KoPIP2;1 protein shared the highest identity (91.26%) with the aquaporin HbPIP2;2, which was isolated from Hevea brasiliensis. Gene expression analysis revealed that the KoPIP2;1 gene was induced higher in leaves than in stems and roots of K. obovata under cold stress. Transient expression of KoPIP2;1 in Nicotiana benthamiana epidermal cells revealed that the KoPIP2;1 protein was localized to the plasma membrane. Overexpressing KoPIP2;1 in Arabidopsis significantly enhanced the lateral root number of the transgenic lines. KoPIP2;1 transgenic Arabidopsis demonstrated better growth, elevated proline content, increased superoxide dismutase (SOD) and peroxidase (POD) activities, and reduced malondialdehyde (MDA) content compared with the wild-type Arabidopsis when exposed to cold stress. The findings suggest that overexpression of KoPIP2;1 probably conferred cold tolerance of transgenic Arabidopsis by enhancing osmoregulation and antioxidant capacity. This present data presents a valuable gene resource that contributes to the advancement of our understanding of aquaporins and their potential application in enhancing plant stress tolerance. |
format | Online Article Text |
id | pubmed-10376877 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-103768772023-07-29 An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana Fei, Jiao Wang, Youshao Cheng, Hao Wang, Hui Wu, Meilin Sun, Fulin Sun, Cuici Bioengineering (Basel) Article Aquaporins (AQPs) are essential channel proteins that play central roles in maintaining water homeostasis. Here, a novel aquaporin gene, named KoPIP2;1, was cloned from the mangrove plant Kandelia obovata by RACE technology. The KoPIP2;1 gene was 1404 bp in length with an open reading frame (ORF) of 852 bp, encoded with 283 amino acids. Database comparisons revealed that KoPIP2;1 protein shared the highest identity (91.26%) with the aquaporin HbPIP2;2, which was isolated from Hevea brasiliensis. Gene expression analysis revealed that the KoPIP2;1 gene was induced higher in leaves than in stems and roots of K. obovata under cold stress. Transient expression of KoPIP2;1 in Nicotiana benthamiana epidermal cells revealed that the KoPIP2;1 protein was localized to the plasma membrane. Overexpressing KoPIP2;1 in Arabidopsis significantly enhanced the lateral root number of the transgenic lines. KoPIP2;1 transgenic Arabidopsis demonstrated better growth, elevated proline content, increased superoxide dismutase (SOD) and peroxidase (POD) activities, and reduced malondialdehyde (MDA) content compared with the wild-type Arabidopsis when exposed to cold stress. The findings suggest that overexpression of KoPIP2;1 probably conferred cold tolerance of transgenic Arabidopsis by enhancing osmoregulation and antioxidant capacity. This present data presents a valuable gene resource that contributes to the advancement of our understanding of aquaporins and their potential application in enhancing plant stress tolerance. MDPI 2023-07-24 /pmc/articles/PMC10376877/ /pubmed/37508905 http://dx.doi.org/10.3390/bioengineering10070878 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Fei, Jiao Wang, Youshao Cheng, Hao Wang, Hui Wu, Meilin Sun, Fulin Sun, Cuici An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana |
title | An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana |
title_full | An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana |
title_fullStr | An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana |
title_full_unstemmed | An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana |
title_short | An Aquaporin Gene (KoPIP2;1) Isolated from Mangrove Plant Kandelia obovata Had Enhanced Cold Tolerance of Transgenic Arabidopsis thaliana |
title_sort | aquaporin gene (kopip2;1) isolated from mangrove plant kandelia obovata had enhanced cold tolerance of transgenic arabidopsis thaliana |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10376877/ https://www.ncbi.nlm.nih.gov/pubmed/37508905 http://dx.doi.org/10.3390/bioengineering10070878 |
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