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Bulletin of Botanical Research ›› 2022, Vol. 42 ›› Issue (5): 811-820.doi: 10.7525/j.issn.1673-5102.2022.05.012

• Molecular biology • Previous Articles     Next Articles

Cloning and Functional Analysis of Heat Shock Protein HbHSP90.8-1 from Hevea brasiliensis Müll. Arg.

Mingyang LIU1, Huaxing XIAO1, Lifeng WANG2, Xiaoxu LIANG1, Yu ZHANG1, Meng WANG1()   

  1. 1.School of Plant Protection,Key Laboratory of Green Prevention and Control of Tropical Plant Diseases and Pests(Hainan University),Ministry of Education,Hainan University,Haikou 570228
    2.Key Laboratory of Biology and Genetic Resources of Rubber Tree,Ministry of Agriculture and Rural Affairs,P. R. China;State Key Laboratory Incubation Base for Cultivation & Physiology of Tropical Crops;Danzhou Investigation & Experiment Station of Tropical Crops,Ministry of Agriculture and Rural Affairs,P. R. China;Rubber Research Institute,Chinese Academy of Tropical Agricultural Sciences,Haikou 571101
  • Received:2021-05-07 Online:2022-09-20 Published:2022-09-15
  • Contact: Meng WANG E-mail:wangmeng@hainanu.edu.cn
  • About author:LIU Mingyang(1996—),female,master,mainly engaged in the research on plant molecular pathology.
  • Supported by:
    National Natural Science Foundation of China(32160370);Earmarked fund for China Agriculture Research System(CARS-33-BC1);High-level Talent Fund of Hainan Province(2019RC164)


Powdery mildew is one of the major leaf diseases in growth of rubber tree. Heat shock protein 90(HSP90) molecular chaperone plays an important role in plant stress resistance. To study the structure of the rubber tree HSP90 family members and their function in powdery mildew resistance, HbHSP90.8-1 was cloned from rubber tree variety Reyan73397 leaf using PCR technology and its structure and function were analyzed by bioinformatics method. The results showed that the cDNA sequence of HbHSP90.8-1 was 2 844 bp in full length, 2 454 bp open reading frame(ORF) and encoded 817 amino acids. HbHSP90.8-1 encoded a stable hydrophilic protein with signal peptide, no transmembrane structure and predicted positioning on endoplasmic reticulum, contained HSP90 superfamily and HATPase superfamily domains. Phylogenetic analysis showed that HbHSP90.8-1 was closely related to MeHSP90, and classified into Jatropha JcHSP90 and Castor RcHSP90. The qRT-PCR analysis showed that HbHSP90.8-1 was expressed in different tissues of rubber tree, and its expression level was the highest in latex. The expression of HbHSP90.8-1 was significantly expressed and up-regulated in leaves treated with Oidium heveae infection, H2O2, ABA and ETH respectively. However, under the treatment of MeJA and SA hormone, the expression of HbHSP90.8-1 showed a downward trend. The study suggested that HbHSP90.8-1 related to the powdery mildew resistance and the hormone signal transduction pathway related to plant disease resistance, and provided a technical guidance for the subsequent study on the molecular regulation mechanism of HbHSP90.8-1 in the powdery mildew resistance in rubber tree.

Key words: rubber tree, powdery mildew, HbHSP90.8-1, bioinformatics, expression analysis

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