Abstract:

Ubiquitination is one of post-translational modifications of plant proteins, which is involved in the regulation of plant growth, development and various stress responses by selective degradation of proteins. The reaction of ubiquitination modification is carried out by the synergistic action of three key enzymes. Ubiquitin molecules are activated by linking to thiol ester bonds of ubiquitin-activating enzymes, and the activated ubiquitin molecules form a complex with ubiquitin-conjugating enzymes, and finally bind to the target protein under the action of ubiquitin-ligase enzymes. With the development of proteomics sequencing technology, the research on ubiquitination modification has become more widespread and deeper. A large number of ubiquitination modified proteins and their modification sites have been identified, which is conducive to further understanding the regulatory mechanism of proteins and further analyzing the function of proteins. In this paper, we mainly introduced the reaction process of the ubiquitin-proteasome system, the structure, quantity and classification of key enzymes of ubiquitination modification, and focused on the functions of ubiquitin-activating enzymes, ubiquitin-binding enzymes and ubiquitin-ligases in plant response to abiotic and biotic stresses. Concurrently, we summarized the issues in studying functions of the key enzymes in plant ubiquitination modification, and discussed the crosstalk between ubiquitination and other modifications, which is of great significance for further research on ubiquitination modification in the field of plant responses to various environmental stresses.

Key words: ubiquitination modification, ubiquitin-activating enzyme, ubiquitin-conjugating enzyme, ubiquitin-ligase enzyme, abiotic stress, biotic stress