Biotechnology Bulletin ›› 2021, Vol. 37 ›› Issue (6): 225-235.doi: 10.13560/j.cnki.biotech.bull.1985.2020-1389

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Low Temperature Stress Response Mediated by Protein Ubiquitination in Plant

WU Feng-zhang(), WANG He-xin   

  1. Institute of Modern Agricultural Research,Dalian University,Dalian 116622
  • Received:2020-11-15 Online:2021-06-26 Published:2021-07-08

Abstract:

Low-temperature stress restricts plant growth,development,and geographical distribution. A large transcriptome reprogramming occurs as a response to low-temperature stress in diverse species,and a number of proteins have been identified as important factors in this adaptive response. Ubiquitination is a post-translational modification that regulates abundance,activities,subcellular compartmentalization and transport,and involved in the low-temperature stress response. The E3 is a major component of the ubiquitin-proteasome system that recognizes the target protein and transfer of ubiquitin from the E2 to the target protein. Owing to its substrate recognition specificity,the E3 regulates various signaling pathways involved in the low-temperature stress response in plants. Therefore,components involved in the ubiquitin-proteasome system are summarized in the present study,and the role of E3 in the low-temperature stress response is described in detail.

Key words: low temperature stress, ubiquitination, E3 ubiquitin ligases, signal transduction, freezing tolerance