Proteomics

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Quantitative proteome analysis of the Arabidopsis thaliana N-degron pathway E3 ligase mutant, prt1-1.

ABSTRACT: The N-degron pathway relates the half-life of a protein to its amino terminal (Nt) residue. Following cleavage of proteins by endopeptidases, new N-t amino acids are revealed and can be recognised by different E3 ligase enzymes that target the substrate proteins for degradation via the proteasome. Studies with artificial proteins have shown that PRT1 is an Arabidopsis thaliana E3 ligase with specificity for aromatic N-termini (phenylalanine, tyrosine, tryptophan), but very little is known about its physiological roles and endogenous substrates. To gain insight into the impact of PRT1 on the proteome, we conducted a quantitative proteomic analysis, comparing leaf proteins from the prt1-1 loss of function mutant with those from wild type plants.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Hongtao Zhang  

LAB HEAD: Hongtao Zhang

PROVIDER: PXD014238 | Pride | 2020-01-09

REPOSITORIES: Pride

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Publications

The <i>Arabidopsis thaliana</i> N-recognin E3 ligase PROTEOLYSIS1 influences the immune response.

Till Christopher J CJ   Vicente Jorge J   Zhang Hongtao H   Oszvald Maria M   Deery Michael J MJ   Pastor Victoria V   Lilley Kathryn S KS   Ray Rumiana V RV   Theodoulou Frederica L FL   Holdsworth Michael J MJ  

Plant direct 20191226 12

N-degron pathways of ubiquitin-mediated proteolysis (formerly known as the N-end rule pathway) control the stability of substrate proteins dependent on the amino-terminal (Nt) residue. Unlike yeast or mammalian N-recognin E3 ligases, which each recognize several different classes of Nt residues, in <i>Arabidopsis thaliana</i>, N-recognin functions of different N-degron pathways are carried out independently by PROTEOLYSIS (PRT)1, PRT6, and other unknown proteins. PRT1 recognizes type 2 aromatic  ...[more]

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