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Review
. 2023 Feb 1;24(3):2750.
doi: 10.3390/ijms24032750.

The Ubiquitin-26S Proteasome Pathway and Its Role in the Ripening of Fleshy Fruits

Affiliations
Review

The Ubiquitin-26S Proteasome Pathway and Its Role in the Ripening of Fleshy Fruits

Wen Jia et al. Int J Mol Sci. .

Abstract

The 26S proteasome is an ATP-dependent proteolytic complex in eukaryotes, which is mainly responsible for the degradation of damaged and misfolded proteins and some regulatory proteins in cells, and it is essential to maintain the balance of protein levels in the cell. The ubiquitin-26S proteasome pathway, which targets a wide range of protein substrates in plants, is an important post-translational regulatory mechanism involved in various stages of plant growth and development and in the maturation process of fleshy fruits. Fleshy fruit ripening is a complex biological process, which is the sum of a series of physiological and biochemical reactions, including the biosynthesis and signal transduction of ripening related hormones, pigment metabolism, fruit texture changes and the formation of nutritional quality. This paper reviews the structure of the 26S proteasome and the mechanism of the ubiquitin-26S proteasome pathway, and it summarizes the function of this pathway in the ripening process of fleshy fruits.

Keywords: 26S proteasome; degradation; ripening of fleshy fruit; ubiquitination.

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Conflict of interest statement

The authors declare that they have no known competing financial interest or personal relationships that could have influenced the work in this paper.

Figures

Figure 1
Figure 1
Structure of the 26S proteasome and the ubiquitin pathway. (A) 20S CP (20S Core Particle); 19S RP (19S Regulatory Particle). (B) Ubiquitination pathway. Ub, ubiquitin; E1, ubiquitin-activating enzyme; E2, ubiquitin-conjugating enzyme; E3 HECT, ubiquitin ligase enzyme with homologous to E6-associated protein C-terminus domain; E3 RING/U-box, ubiquitin ligase enzyme with really interesting new gene/U-box domain; S, substrate protein.
Figure 2
Figure 2
The function of the ubiquitin–26S proteasome pathway in ethylene biosynthesis and signal transduction pathway. S: substrate proteins, such as SlREM1, MaMADS1, MdbHLH3, MaACO1, MaNAC2, MaACS1, CsACS2, and CsSF1.
Figure 3
Figure 3
The function of the ubiquitin–26S proteasome pathway in pigment metabolism. S: substrate proteins, such as SlBBX20, PSY1 precursor protein, ClLCYB, SlREM1, TOX complex, MdBEL7, SlGLK2, SlBMD5, MdCOP1, MdBT2, MdMYB1, PacMYBA, PpbHLH64, MdMYB308L, MdTCP46, and MdBBX22.

References

    1. Xu D.D., Sun F., Wang Y.X., Shi Y.Y., Wang W.S., Fu B.Y. Biological function insights into the ubiquitin/26S proteasome pathway in rice. J. Agric. Sci. Technol. 2018;20:25–33.
    1. Collins G.A., Goldberg A.L. The logic of the 26S proteasome. Cell. 2017;169:792–806. doi: 10.1016/j.cell.2017.04.023. - DOI - PMC - PubMed
    1. Seeger M., Ferrell K., Dubiel W. The 26S proteasome: A dynamic structure. Mol. Biol. Rep. 1997;24:83–88. doi: 10.1023/A:1006837600040. - DOI - PubMed
    1. Yang P.Z., Fu H.Y., Walker J., Papa C.M., Smalle J., Ju Y.M., Vierstra R.D. Purification of the Arabidopsis 26S proteasome: Biochemical and molecular analyses revealed the presence of multiple isoforms. J. Biol. Chem. 2004;279:6401–6413. doi: 10.1074/jbc.M311977200. - DOI - PubMed
    1. Pickart C.M., Fushman D. Polyubiquitin chains: Polymeric protein signals. Curr. Opin. Chem. Biol. 2008;8:610–616. doi: 10.1016/j.cbpa.2004.09.009. - DOI - PubMed

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