Abstract

E3 ubiquitin ligases of the ubiquitin proteasome system (UPS) mediate recognition of substrates and later transfer the ubiquitin (Ub). They are the most expanded components of the system. The Really Interesting New Gene (RING) domain contains 40–60 residues that are highly represented among E3 ubiquitin ligases. The Arabidopsis thaliana E3 ubiquitin ligases with a RING finger primarily contain RING-HC or RING-H2 type domains or less frequently RING-v, RING-C2, RING-D, RING-S/T and RING-G type domains. Our previous work on three E3 ubiquitin ligase families with a RING-H2 type domain, ATL, BTL, and CTL, suggested that a phylogenetic distribution based on the RING domain allowed for the creation a catalog of known domains or unknown conserved motifs. This work provided a useful and comprehensive view of particular families of RING E3 ubiquitin ligases. We updated the annotation of A. thaliana RING proteins and surveyed RING proteins from 30 species across eukaryotes. Based on domain architecture profile of the A. thaliana proteins, we catalogued 4711 RING finger proteins into 107 groups, including 66 previously described gene families or single genes and 36 novel families or undescribed genes. Forty-four groups were specific to a plant lineage while 41 groups consisted of proteins found in all eukaryotic species. Our present study updates the current classification of plant RING finger proteins and reiterates the importance of these proteins in plant growth and adaptation.

Highlights

  • Protein modifications result in a diversification of their function

  • Most of them are assigned to two main classes, Really Interesting New Gene (RING)-H2 and RING-HC, and the remainder are allocated to five less abundant classes

  • We have previously based our survey of ATL, BZF ATLs (BTLs), and CTL RING finger protein families on the layout of residues located at the RING domain followed by the inspection of transmembrane helices, YELL, or the GLD conserved motif

Read more

Summary

Introduction

Protein modifications result in a diversification of their function. August 31, 2018 plant RING E3 ubiquitin ligases cellular protein repertoire. An array of Ub-dependent targets are degraded by the 26S proteasome, including receptors, transcription factors, metabolic enzymes and misfolded proteins which unveils the compelling function of ubiquitination. Non-degradative pathways result in either the activation of key signaling factors, endocytosis, or in the control of gene expression by modifying histone proteins [3]. Specific types of Ub modification govern the fate of ubiquitinated target proteins. Monoubiquitination promotes endocytosis, Lys6-linked poly-Ub chains serve to control DNA repair processes (mainly Lys48-linked and Lys11-linked poly-Ub chains degraded by the 26S proteasome), and Lys63-linked poly-Ub chains serve in protein activation [4, 5]

Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call