Welcome to Bulletin of Botanical Research! Today is Share:

Bulletin of Botanical Research ›› 2023, Vol. 43 ›› Issue (4): 622-630.doi: 10.7525/j.issn.1673-5102.2023.04.015

• Molecular biology • Previous Articles     Next Articles

Cloning and Functional Analysis of Deubiquitinating Enzyme Gene UCHs from Hevea brasiliensis

Mingyue YUAN1,2, Tianzhong ZHOU2,3, Ma YU1, Bin HU2, Xiangyu LONG2, Hua CHEN1()   

  1. 1.School of Life Science and Engineering,Southwest University of Science and Technology,Mianyang 621010
    2.Rubber Research Institute,Chinese Academy of Tropical Agricultural Sciences/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,CATAS,Haikou 571101
    3.Pu'er University,Yunnan Agricultural University,Puer 665099
  • Received:2023-03-19 Online:2023-07-20 Published:2023-07-03
  • Contact: Hua CHEN E-mail:hchen@swust.edu.cn
  • About author:YUAN Mingyue(1998—),female,master student,molecular biology of rubber production from rubber trees.
  • Supported by:
    Project of National Natural Science Foundation of China(31971680);Innovation Team Project of Hainan Natural Science Foundation(322CXTD526);Special Project of Basic Research Funds for Public Welfare Research Institutes of the Central Government(1630022022009);Southwest University of Science and Technology,PhD Foundation Project(19ZX7117)

Abstract:

To investigate the potential function of ubiquitin carboxyl terminal hydrolases(UCHs) in the ubiquitination process of laticiferous of Hevea brasiliensis, the full-length sequences of two UCHs family members(HbUCH-L3 and HbUCH-L5) were isolated from Hevea brasiliensis, and both had typical UCHs domains. The open reading frame of HbUCH-L3 and HbUCH-L5 were 993 bp and 558 bp, and encoded 330 and 185 amino acids, respectively. The results of qRT-PCR showed that HbUCH-L3 and HbUCH-L5 were constitutively expressed in all tissues, but was low in latex. In vitro ubiquitination substrates cleavage of recombinant HbUCHs showed that both HbUCH-L3 and HbUCH-L5 had the function of hydrolyzing ubiquitin. HbUCHs significantly reduced the overall ubiquitination level of C-serum proteins; while, the deubiquitinating activity of HbUCH-L3 was higher than that of HbUCH-L5. Therefore, it was speculated that UCHs played a role in maintaining the dynamic balance of laticiferous ubiquitination and thus played a specific biological function, but the exact mechanism was still unclear.

Key words: Hevea brasiliensis, ubiquitin carboxy-terminal hydrolases, laticiferous ubiquitination, in vitro ubiquitination substrate cleavage

CLC Number: