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Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana
Background. Water channel proteins, also called aquaporins, are integral membrane proteins from major intrinsic protein (MIP) family and involved in several pathways including not only water transport but also cell signaling, reproduction, and photosynthesis. The full cDNA and protein sequences of a...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5023841/ https://www.ncbi.nlm.nih.gov/pubmed/27689074 http://dx.doi.org/10.1155/2016/2483258 |
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author | Li, Ming Liang, Zhaoxu Di, Cuixia Fang, Weikuan Wu, Kaichao Chen, Maoshan He, Shanshan Zeng, Yuan Jing, Yan Liang, Jun Tan, Fang Li, Song Chen, Tuo Liu, Guangxiu An, Lizhe |
author_facet | Li, Ming Liang, Zhaoxu Di, Cuixia Fang, Weikuan Wu, Kaichao Chen, Maoshan He, Shanshan Zeng, Yuan Jing, Yan Liang, Jun Tan, Fang Li, Song Chen, Tuo Liu, Guangxiu An, Lizhe |
author_sort | Li, Ming |
collection | PubMed |
description | Background. Water channel proteins, also called aquaporins, are integral membrane proteins from major intrinsic protein (MIP) family and involved in several pathways including not only water transport but also cell signaling, reproduction, and photosynthesis. The full cDNA and protein sequences of aquaporin in Chorispora bungeana Fisch. & C.A. Mey (C. bungeana) are still unknown. Results. In this study, PCR and rapid amplification of cDNA ends approaches were used to clone the full cDNA of LRB7 (GenBank accession number: EU636988) of C. bungeana. Sequence analysis indicated that it was 1235 bp, which had two introns and encoded a protein of 250 amino acids. Structure analysis revealed that the protein had two conserved NPA motifs, one of which is MIP signature sequence (SGxHxNPAVT), six membrane helix regions, and additional membrane-embedded domains. Phylogenetic analysis suggested that the protein was from TIP2 subgroup. Surprisingly, semiquantitative RT-PCR experiment and western blot analysis showed that LRB7 and TIP2 were only detectable in roots, unlike Arabidopsis and Raphanus. Connecting with our previous studies, LRB7 was supported to associate with chilling-tolerance in C. bungeana. Conclusion. This is the first time to characterize the full sequences of LRB7 gene and water channel protein in C. bungeana. Our findings contribute to understanding the water transports in plants under low temperatures. |
format | Online Article Text |
id | pubmed-5023841 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-50238412016-09-29 Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana Li, Ming Liang, Zhaoxu Di, Cuixia Fang, Weikuan Wu, Kaichao Chen, Maoshan He, Shanshan Zeng, Yuan Jing, Yan Liang, Jun Tan, Fang Li, Song Chen, Tuo Liu, Guangxiu An, Lizhe Biomed Res Int Research Article Background. Water channel proteins, also called aquaporins, are integral membrane proteins from major intrinsic protein (MIP) family and involved in several pathways including not only water transport but also cell signaling, reproduction, and photosynthesis. The full cDNA and protein sequences of aquaporin in Chorispora bungeana Fisch. & C.A. Mey (C. bungeana) are still unknown. Results. In this study, PCR and rapid amplification of cDNA ends approaches were used to clone the full cDNA of LRB7 (GenBank accession number: EU636988) of C. bungeana. Sequence analysis indicated that it was 1235 bp, which had two introns and encoded a protein of 250 amino acids. Structure analysis revealed that the protein had two conserved NPA motifs, one of which is MIP signature sequence (SGxHxNPAVT), six membrane helix regions, and additional membrane-embedded domains. Phylogenetic analysis suggested that the protein was from TIP2 subgroup. Surprisingly, semiquantitative RT-PCR experiment and western blot analysis showed that LRB7 and TIP2 were only detectable in roots, unlike Arabidopsis and Raphanus. Connecting with our previous studies, LRB7 was supported to associate with chilling-tolerance in C. bungeana. Conclusion. This is the first time to characterize the full sequences of LRB7 gene and water channel protein in C. bungeana. Our findings contribute to understanding the water transports in plants under low temperatures. Hindawi Publishing Corporation 2016 2016-09-01 /pmc/articles/PMC5023841/ /pubmed/27689074 http://dx.doi.org/10.1155/2016/2483258 Text en Copyright © 2016 Ming Li et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Li, Ming Liang, Zhaoxu Di, Cuixia Fang, Weikuan Wu, Kaichao Chen, Maoshan He, Shanshan Zeng, Yuan Jing, Yan Liang, Jun Tan, Fang Li, Song Chen, Tuo Liu, Guangxiu An, Lizhe Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana |
title | Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana
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title_full | Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana
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title_fullStr | Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana
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title_full_unstemmed | Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana
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title_short | Molecular Characterization of LRB7 Gene and a Water Channel Protein TIP2 in Chorispora bungeana
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title_sort | molecular characterization of lrb7 gene and a water channel protein tip2 in chorispora bungeana |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5023841/ https://www.ncbi.nlm.nih.gov/pubmed/27689074 http://dx.doi.org/10.1155/2016/2483258 |
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