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作 者:Zeyuan Liu Ningning Bian Jianyan Guo Shuang Zhao Abid Khan Baohua Chu Ziqing Ma Chundong Niu Fengwang Ma Ming Ma Qingmei Guan Xuewei Li
机构地区:[1]State Key Laboratory of Crop Stress Biology for Arid Areas/Shaanxi Key Laboratory of Apple,College of Horticulture,Northwest A&F University,Yangling 712100,Shaanxi,China [2]Department of Horticulture,The University of Haripur,Haripur 22620,Pakistan [3]Gansu Academy of Agricultural Sciences,Lanzhou 730000,Gansu,China
出 处:《Stress Biology》2023年第1期114-125,共12页逆境生物学(英文)
基 金:supported by the National Key Research and Development Project(2022YFD1602107);the Key S&T Special Projects of Shaanxi Province,China(2020zdzx03-01-02);the Natural Science Foundation of Shaanxi Province,China(2022JQ-179).
摘 要:Heat stress,which is caused by global warming,threatens crops yield and quality across the world.As a kind of post-translation modification,SUMOylation involves in plants heat stress response with a rapid and wide pattern.Here,we identified small ubiquitin modifiers(SUMO),which affect drought tolerance in apple,also participated in thermotolerance.Six isoforms of SUMOs located on six chromosomes in apple genome,and all the SUMOs were up-regulated in response to heat stress condition.The MdSUMO2 RNAi transgenic apple plants exhibited higher survival rate,lower ion leakage,higher catalase(CAT)activity,and Malondialdehyde(MDA)content under heat stress.MdDREB2A,the substrate of MdSUMO2 in apple,was accumulated in MdSUMO2 RNAi transgenic plants than the wild type GL-3 at the protein level in response to heat stress treatment.Further,the inhibited SUMOylation level of MdDREB2A in MdSUMO2 RNAi plants might repress its ubiquitination,too.The accumulated MdDREB2A in MdSUMO2 RNAi plants further induced heat-responsive genes expression to strengthen plants thermotolerance,including MdHSFA3,MdHSP26.5,MdHSP18.2,MdHSP70,MdCYP18-1 and MdTLP1.In summary,these findings illustrate that interfering small ubiquitin modifiers(SUMO)in apple improves plants thermotolerance,partly by facilitating the stability and activity of MdDREB2A.
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