6lhn
From Proteopedia
RLGSGG-AtPRT6 UBR box
Structural highlights
FunctionPRT6_ARATH Ubiquitin protein ligase which is a component of the N-end rule pathway with arginine specificity, and functions with the arginyltransferases ATE1 and ATE2. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed:17572409, PubMed:19255443, PubMed:19620738, PubMed:22020282). Does not participate in degradation of proteins with N-terminal Phe or Leu (PubMed:17572409). The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination (PubMed:19255443). The N-end rule pathway regulates various aspects of leaf and shoot development (PubMed:19620738). Involved in the ubiquitination and subsequent degradation of RAP2-12, an activator of hypoxic gene expression. The ubiquitination occurs after the N-arginylation of RAP2-12 by ATE1 or ATE2 under aerobic conditions (PubMed:22020282). The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato (PubMed:27173012, PubMed:30117535). Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity (PubMed:27173012). Controls the expression of specific defense-response genes, activates the synthesis pathway for the phytoalexin camalexin, and influences basal resistance to the hemibiotroph pathogen Pseudomonas syringae pv tomato (PubMed:30117535). Coordinates the mobilization of seed storage reserves and regulates the abundance and activities of several proteases following seed germination (PubMed:29168982).[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedThe N-degron pathway, formerly the N-end rule pathway, is a protein degradation process that determines the half-life of proteins based on their N-terminal residues. In contrast to the well-established in vivo studies over decades, in vitro studies of this pathway, including biochemical characterization and high-resolution structures, are relatively limited. In this study, we have developed a unique fusion technique using microtubule-associated protein 1A/1B light chain 3B, a key marker protein of autophagy, to tag the N-terminus of the proteins involved in the N-degron pathway, which enables high yield of homogeneous target proteins with variable N-terminal residues for diverse biochemical studies including enzymatic and binding assays and substrate identification. Intriguingly, crystallization showed a markedly enhanced probability, even for the N-degron complexes. To validate our results, we determined the structures of select proteins in the N-degron pathway and compared them to the PDB-deposited proteins. Furthermore, several biochemical applications of this technique were introduced. Therefore, this technique can be used as a general tool for the in vitro study of the N-degron pathway. Use of the LC3B-fusion technique for biochemical and structural studies of proteins involved in the N-degron pathway.,Kim L, Kwon DH, Heo J, Park MR, Song HK J Biol Chem. 2020 Jan 9. pii: RA119.010912. doi: 10.1074/jbc.RA119.010912. PMID:31919097[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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