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A novel α/β-hydrolase gene IbMas enhances salt tolerance in transgenic sweetpotato.

Liu D, Wang L, Zhai H, Song X, He S, Liu Q - PLoS ONE (2014)

Bottom Line: Shangshu 19) plants exhibited significantly higher salt tolerance compared with the wild-type.Proline content was significantly increased, whereas malonaldehyde content was significantly decreased in the transgenic plants.H2O2 was also found to be significantly less accumulated in the transgenic plants than in the wild-type.

View Article: PubMed Central - PubMed

Affiliation: Beijing Key Laboratory of Crop Genetic Improvement/Laboratory of Crop Heterosis and Utilization, Ministry of Education, China Agricultural University, Beijing, China.

ABSTRACT
Salt stress is one of the major environmental stresses in agriculture worldwide and affects crop productivity and quality. The development of crops with elevated levels of salt tolerance is therefore highly desirable. In the present study, a novel maspardin gene, named IbMas, was isolated from salt-tolerant sweetpotato (Ipomoea batatas (L.) Lam.) line ND98. IbMas contains maspardin domain and belongs to α/β-hydrolase superfamily. Expression of IbMas was up-regulated in sweetpotato under salt stress and ABA treatment. The IbMas-overexpressing sweetpotato (cv. Shangshu 19) plants exhibited significantly higher salt tolerance compared with the wild-type. Proline content was significantly increased, whereas malonaldehyde content was significantly decreased in the transgenic plants. The activities of superoxide dismutase (SOD) and photosynthesis were significantly enhanced in the transgenic plants. H2O2 was also found to be significantly less accumulated in the transgenic plants than in the wild-type. Overexpression of IbMas up-regulated the salt stress responsive genes, including pyrroline-5-carboxylate synthase, pyrroline-5-carboxylate reductase, SOD, psbA and phosphoribulokinase genes, under salt stress. These findings suggest that overexpression of IbMas enhances salt tolerance of the transgenic sweetpotato plants by regulating osmotic balance, protecting membrane integrity and photosynthesis and increasing reactive oxygen species scavenging capacity.

No MeSH data available.


Sequence alignment of IbMas protein with its homologous proteins from various plant species.The proteins are as follows: XP_006363736 from Solanum tuberosum, XP_007039974 from Theobroma cacao, XP_002267811 from Vitis vinifera, XP_004245715 from Solanum lycopersicum, EXC17874 from Morus notabilis, XP_006368699 from Populus trichocarpa, KDP25601 from Jatropha curcas and XP_002509605 from Ricinus communis. The maspardin domain is marked by asterisk line.
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pone-0115128-g001: Sequence alignment of IbMas protein with its homologous proteins from various plant species.The proteins are as follows: XP_006363736 from Solanum tuberosum, XP_007039974 from Theobroma cacao, XP_002267811 from Vitis vinifera, XP_004245715 from Solanum lycopersicum, EXC17874 from Morus notabilis, XP_006368699 from Populus trichocarpa, KDP25601 from Jatropha curcas and XP_002509605 from Ricinus communis. The maspardin domain is marked by asterisk line.

Mentions: The IbMas gene was cloned from salt-tolerant sweetpotato line ND98 by RACE and submitted to GenBank (accession no. KM095957). The cDNA sequence of 1564 bp contained an 1233 bp open reading frame (ORF) encoding a 410 amino acids polypeptide with a molecular weight of 45.4 kDa and an isoelectric point (pI) of 6.27. Sequence analysis via InterPro program (http://www.ebi.ac.uk/interpro/) showed that IbMas protein contained typical maspardin domain and belonged to α/β-hydrolase superfamily (Fig. 1). A BLASTX search indicated that no homolog of known function was similar to IbMas in plants, while the amino acid sequence of IbMas showed 66.99% to 71.53% amino acid identity with predicted protein products of XP_002509605 from Ricinus communis, KDP25601 from Jatropha curcas, XP_006368699 from Populus trichocarpa, EXC17874 from Morus notabilis, XP_004245715 from Solanum lycopersicum, XP_002267811 from Vitis vinifera, XP_007039974 from Theobroma cacao and XP_006363736 from Solanum tuberosum. Phylogenetic analysis revealed that IbMas had a close relationship with predicted protein products of XP_006363736 from Solanum tuberosum and XP_004245715 from Solanum lycopersicum (Fig. 2).


A novel α/β-hydrolase gene IbMas enhances salt tolerance in transgenic sweetpotato.

Liu D, Wang L, Zhai H, Song X, He S, Liu Q - PLoS ONE (2014)

Sequence alignment of IbMas protein with its homologous proteins from various plant species.The proteins are as follows: XP_006363736 from Solanum tuberosum, XP_007039974 from Theobroma cacao, XP_002267811 from Vitis vinifera, XP_004245715 from Solanum lycopersicum, EXC17874 from Morus notabilis, XP_006368699 from Populus trichocarpa, KDP25601 from Jatropha curcas and XP_002509605 from Ricinus communis. The maspardin domain is marked by asterisk line.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4264881&req=5

pone-0115128-g001: Sequence alignment of IbMas protein with its homologous proteins from various plant species.The proteins are as follows: XP_006363736 from Solanum tuberosum, XP_007039974 from Theobroma cacao, XP_002267811 from Vitis vinifera, XP_004245715 from Solanum lycopersicum, EXC17874 from Morus notabilis, XP_006368699 from Populus trichocarpa, KDP25601 from Jatropha curcas and XP_002509605 from Ricinus communis. The maspardin domain is marked by asterisk line.
Mentions: The IbMas gene was cloned from salt-tolerant sweetpotato line ND98 by RACE and submitted to GenBank (accession no. KM095957). The cDNA sequence of 1564 bp contained an 1233 bp open reading frame (ORF) encoding a 410 amino acids polypeptide with a molecular weight of 45.4 kDa and an isoelectric point (pI) of 6.27. Sequence analysis via InterPro program (http://www.ebi.ac.uk/interpro/) showed that IbMas protein contained typical maspardin domain and belonged to α/β-hydrolase superfamily (Fig. 1). A BLASTX search indicated that no homolog of known function was similar to IbMas in plants, while the amino acid sequence of IbMas showed 66.99% to 71.53% amino acid identity with predicted protein products of XP_002509605 from Ricinus communis, KDP25601 from Jatropha curcas, XP_006368699 from Populus trichocarpa, EXC17874 from Morus notabilis, XP_004245715 from Solanum lycopersicum, XP_002267811 from Vitis vinifera, XP_007039974 from Theobroma cacao and XP_006363736 from Solanum tuberosum. Phylogenetic analysis revealed that IbMas had a close relationship with predicted protein products of XP_006363736 from Solanum tuberosum and XP_004245715 from Solanum lycopersicum (Fig. 2).

Bottom Line: Shangshu 19) plants exhibited significantly higher salt tolerance compared with the wild-type.Proline content was significantly increased, whereas malonaldehyde content was significantly decreased in the transgenic plants.H2O2 was also found to be significantly less accumulated in the transgenic plants than in the wild-type.

View Article: PubMed Central - PubMed

Affiliation: Beijing Key Laboratory of Crop Genetic Improvement/Laboratory of Crop Heterosis and Utilization, Ministry of Education, China Agricultural University, Beijing, China.

ABSTRACT
Salt stress is one of the major environmental stresses in agriculture worldwide and affects crop productivity and quality. The development of crops with elevated levels of salt tolerance is therefore highly desirable. In the present study, a novel maspardin gene, named IbMas, was isolated from salt-tolerant sweetpotato (Ipomoea batatas (L.) Lam.) line ND98. IbMas contains maspardin domain and belongs to α/β-hydrolase superfamily. Expression of IbMas was up-regulated in sweetpotato under salt stress and ABA treatment. The IbMas-overexpressing sweetpotato (cv. Shangshu 19) plants exhibited significantly higher salt tolerance compared with the wild-type. Proline content was significantly increased, whereas malonaldehyde content was significantly decreased in the transgenic plants. The activities of superoxide dismutase (SOD) and photosynthesis were significantly enhanced in the transgenic plants. H2O2 was also found to be significantly less accumulated in the transgenic plants than in the wild-type. Overexpression of IbMas up-regulated the salt stress responsive genes, including pyrroline-5-carboxylate synthase, pyrroline-5-carboxylate reductase, SOD, psbA and phosphoribulokinase genes, under salt stress. These findings suggest that overexpression of IbMas enhances salt tolerance of the transgenic sweetpotato plants by regulating osmotic balance, protecting membrane integrity and photosynthesis and increasing reactive oxygen species scavenging capacity.

No MeSH data available.