Abstract
E3 ubiquitin ligases are the most expanded components of the ubiquitin proteasome system (UPS). They mediate the recognition of substrates and later transfer the ubiquitin (Ub) of the system. Really Interesting New Gene (RING) finger proteins characterized by the RING domain, which contains 40–60 residues, are thought to be E3 ubiquitin ligase. RING-finger proteins play significant roles in plant growth, stress resistance, and signal transduction. In this study, we mainly describe the structural characteristics, classifications, and subcellular localizations of RING-finger proteins, as well the physiological processes of RING-finger proteins in plant growth and development. We also summarize the functions of plant RING-finger proteins in plant stress resistance. Finally, further research on plant RING-finger proteins is suggested, thereby establishing a strong foundation for the future study of plant RING-finger proteins.
Highlights
Proteins diversify their functions needed for different modifications
When the brassinosteroid-responsive Really Interesting New Gene (RING)-H2 (BRH1) gene in Arabidopsis thaliana is overexpressed, the rosette leaves of the transgenic lines were extremely curled, suggesting that it may be involved in the Brassinosteroid (BR) signaling pathway to regulate the shape of the leaves [35]
The RING-finger protein MYB30-interacting E3 ligase 1 (MIEL1) in Arabidopsis thaliana acts as an E3 ligase ubiquitinating transcription factor Myb domain protein 30 (MYB30) and degrades transgenic MYB30, thereby reducing the expression of disease-resistant genes and reducing the plant’s immune response [44]
Summary
Proteins diversify their functions needed for different modifications. Ubiquitin (Ub) is a protein consisting of 76 amino acids that is known as a post-translational protein modifier in all eukaryotes that affect the fate of the protein. In all of these loop variants, the substituted amino acids can participate in the Zn2+ connection, so the global three-dimensional structure of the domain is conserved [11] These characteristics facilitate the classification of RING-finger proteins based on their domain architectures [8,9]. There are 477 RING domains detected from 469 predicted proteins in the whole Arabidopsis thaliana proteome These members are mainly divided into seven subtypes according to structural differences: RING-H2(241), RING-HC(186), RING-v(25), RING-C2(10), RING-D(10), RING-S/T(4), and RING-G(1). Other RING-finger types differ mainly in the spacing between the ML or the position of one or more metal ligands (Figure 2) The majority of these RING-finger proteins have been proven to possess E3 activity by ubiquitination essays in vitro, even the RING-finger proteins with substituted zinc binding acid residues or with slightly altered spacing [9,13,14]. The shape pentagons represent the Zn+; the red letter represents the conserved amino acid residue, and X stands for any amino acid
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