Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress
The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum...
Ausführliche Beschreibung
Autor*in: |
Jun Wang [verfasserIn] Xin Gao [verfasserIn] Jun Dong [verfasserIn] Xinyu Tian [verfasserIn] Junzhe Wang [verfasserIn] Jairo A. Palta [verfasserIn] Shengbao Xu [verfasserIn] Yan Fang [verfasserIn] Zhonghua Wang [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Übergeordnetes Werk: |
In: Frontiers in Plant Science - Frontiers Media S.A., 2011, 11(2020) |
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Übergeordnetes Werk: |
volume:11 ; year:2020 |
Links: |
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DOI / URN: |
10.3389/fpls.2020.00243 |
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Katalog-ID: |
DOAJ029299527 |
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10.3389/fpls.2020.00243 doi (DE-627)DOAJ029299527 (DE-599)DOAJdc5eb36dc425453c9c80c39a7b218314 DE-627 ger DE-627 rakwb eng SB1-1110 Jun Wang verfasserin aut Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. TaHSP23.9 small heat shock protein heat stress salt stress wheat (Triticum aestivum L.) Arabidopsis (Arabidopsis thaliana) Plant culture Xin Gao verfasserin aut Jun Dong verfasserin aut Xinyu Tian verfasserin aut Junzhe Wang verfasserin aut Jairo A. Palta verfasserin aut Jairo A. Palta verfasserin aut Shengbao Xu verfasserin aut Yan Fang verfasserin aut Zhonghua Wang verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 11(2020) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:11 year:2020 https://doi.org/10.3389/fpls.2020.00243 kostenfrei https://doaj.org/article/dc5eb36dc425453c9c80c39a7b218314 kostenfrei https://www.frontiersin.org/article/10.3389/fpls.2020.00243/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 |
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10.3389/fpls.2020.00243 doi (DE-627)DOAJ029299527 (DE-599)DOAJdc5eb36dc425453c9c80c39a7b218314 DE-627 ger DE-627 rakwb eng SB1-1110 Jun Wang verfasserin aut Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. TaHSP23.9 small heat shock protein heat stress salt stress wheat (Triticum aestivum L.) Arabidopsis (Arabidopsis thaliana) Plant culture Xin Gao verfasserin aut Jun Dong verfasserin aut Xinyu Tian verfasserin aut Junzhe Wang verfasserin aut Jairo A. Palta verfasserin aut Jairo A. Palta verfasserin aut Shengbao Xu verfasserin aut Yan Fang verfasserin aut Zhonghua Wang verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 11(2020) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:11 year:2020 https://doi.org/10.3389/fpls.2020.00243 kostenfrei https://doaj.org/article/dc5eb36dc425453c9c80c39a7b218314 kostenfrei https://www.frontiersin.org/article/10.3389/fpls.2020.00243/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 |
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10.3389/fpls.2020.00243 doi (DE-627)DOAJ029299527 (DE-599)DOAJdc5eb36dc425453c9c80c39a7b218314 DE-627 ger DE-627 rakwb eng SB1-1110 Jun Wang verfasserin aut Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. TaHSP23.9 small heat shock protein heat stress salt stress wheat (Triticum aestivum L.) Arabidopsis (Arabidopsis thaliana) Plant culture Xin Gao verfasserin aut Jun Dong verfasserin aut Xinyu Tian verfasserin aut Junzhe Wang verfasserin aut Jairo A. Palta verfasserin aut Jairo A. Palta verfasserin aut Shengbao Xu verfasserin aut Yan Fang verfasserin aut Zhonghua Wang verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 11(2020) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:11 year:2020 https://doi.org/10.3389/fpls.2020.00243 kostenfrei https://doaj.org/article/dc5eb36dc425453c9c80c39a7b218314 kostenfrei https://www.frontiersin.org/article/10.3389/fpls.2020.00243/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 |
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10.3389/fpls.2020.00243 doi (DE-627)DOAJ029299527 (DE-599)DOAJdc5eb36dc425453c9c80c39a7b218314 DE-627 ger DE-627 rakwb eng SB1-1110 Jun Wang verfasserin aut Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. TaHSP23.9 small heat shock protein heat stress salt stress wheat (Triticum aestivum L.) Arabidopsis (Arabidopsis thaliana) Plant culture Xin Gao verfasserin aut Jun Dong verfasserin aut Xinyu Tian verfasserin aut Junzhe Wang verfasserin aut Jairo A. Palta verfasserin aut Jairo A. Palta verfasserin aut Shengbao Xu verfasserin aut Yan Fang verfasserin aut Zhonghua Wang verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 11(2020) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:11 year:2020 https://doi.org/10.3389/fpls.2020.00243 kostenfrei https://doaj.org/article/dc5eb36dc425453c9c80c39a7b218314 kostenfrei https://www.frontiersin.org/article/10.3389/fpls.2020.00243/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 |
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SB1-1110 Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress TaHSP23.9 small heat shock protein heat stress salt stress wheat (Triticum aestivum L.) Arabidopsis (Arabidopsis thaliana) |
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Over-Expression of the Heat-Responsive Wheat Gene TaHSP23.9 in Transgenic Arabidopsis Conferred Tolerance to Heat and Salt Stress |
abstract |
The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. |
abstractGer |
The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. |
abstract_unstemmed |
The small heat shock proteins (sHSP) are stress-induced proteins with molecular weights ranging from 12 to 42 kDa that act as molecular chaperones to prevent the irreversible aggregation of denaturing proteins. In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties. |
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In this study, we cloned the heat responsive gene TaHSP23.9 from wheat (Triticum aestivum) based on TMT-labeled quantitative proteomic analysis in our previous work and examined its function in the response of transgenic Arabidopsis to heat and salt stress. Amino acid alignment and phylogenetic tree analysis showed that TaHSP23.9 contained a typically conserved structure of the alpha-crystallin domain and is closely related to OsHSP23.2 in rice. Transient expression assays demonstrated that TaHSP23.9 is located on the endoplasmic reticulum. Quantitative real-time PCR demonstrated that TaHSP23.9 was expressed much more in filling grains under normal conditions and was significantly upregulated by heat and salt stress. Transgenic Arabidopsis plants that constitutively over-expressed TaHSP23.9 had no visible differences or adverse phenotypes compared with the wild type under normal conditions but exhibited enhanced tolerance to heat and salt stress under stress conditions. In addition, we found that the expression level of TaHSP23.9 was significantly higher in the heat-tolerant wheat varieties than in the heat-sensitive varieties. Our results suggest that TaHSP23.9 may function as a protein chaperone to positively regulate plant responses to heat and salt stress and could be developed as a molecular marker for screening heat-tolerant wheat varieties.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">TaHSP23.9</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">small heat shock protein</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">heat stress</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">salt stress</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">wheat (Triticum aestivum L.)</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Arabidopsis (Arabidopsis thaliana)</subfield></datafield><datafield tag="653" ind1=" " ind2="0"><subfield code="a">Plant culture</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Xin Gao</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Jun Dong</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Xinyu Tian</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Junzhe Wang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Jairo A. 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