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The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response

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...

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Autores principales: Till, Christopher J., Vicente, Jorge, Zhang, Hongtao, Oszvald, Maria, Deery, Michael J., Pastor, Victoria, Lilley, Kathryn S., Ray, Rumiana V., Theodoulou, Frederica L., Holdsworth, Michael J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6933115/
https://www.ncbi.nlm.nih.gov/pubmed/31891113
http://dx.doi.org/10.1002/pld3.194
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author Till, Christopher J.
Vicente, Jorge
Zhang, Hongtao
Oszvald, Maria
Deery, Michael J.
Pastor, Victoria
Lilley, Kathryn S.
Ray, Rumiana V.
Theodoulou, Frederica L.
Holdsworth, Michael J.
author_facet Till, Christopher J.
Vicente, Jorge
Zhang, Hongtao
Oszvald, Maria
Deery, Michael J.
Pastor, Victoria
Lilley, Kathryn S.
Ray, Rumiana V.
Theodoulou, Frederica L.
Holdsworth, Michael J.
author_sort Till, Christopher J.
collection PubMed
description 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 Arabidopsis thaliana, 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 Nt‐destabilizing residues and PRT6 recognizes type 1 basic residues. These two N‐recognin functions diverged as separate proteins early in the evolution of plants, before the conquest of the land. We demonstrate that loss of PRT1 function promotes the plant immune system, as mutant prt1‐1 plants showed greater apoplastic resistance than WT to infection by the bacterial hemi‐biotroph Pseudomonas syringae pv tomato (Pst) DC3000. Quantitative proteomics revealed increased accumulation of proteins associated with specific components of plant defense in the prt1‐1 mutant, concomitant with increased accumulation of salicylic acid. The effects of the prt1 mutation were additional to known effects of prt6 in influencing the immune system, in particular, an observed over‐accumulation of pipecolic acid (Pip) in the double‐mutant prt1‐1 prt6‐1. These results demonstrate a potential role for PRT1 in controlling aspects of the plant immune system and suggest that PRT1 limits the onset of the defense response via degradation of substrates with type 2 Nt‐destabilizing residues.
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spelling pubmed-69331152019-12-30 The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response Till, Christopher J. Vicente, Jorge Zhang, Hongtao Oszvald, Maria Deery, Michael J. Pastor, Victoria Lilley, Kathryn S. Ray, Rumiana V. Theodoulou, Frederica L. Holdsworth, Michael J. Plant Direct Original Research 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 Arabidopsis thaliana, 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 Nt‐destabilizing residues and PRT6 recognizes type 1 basic residues. These two N‐recognin functions diverged as separate proteins early in the evolution of plants, before the conquest of the land. We demonstrate that loss of PRT1 function promotes the plant immune system, as mutant prt1‐1 plants showed greater apoplastic resistance than WT to infection by the bacterial hemi‐biotroph Pseudomonas syringae pv tomato (Pst) DC3000. Quantitative proteomics revealed increased accumulation of proteins associated with specific components of plant defense in the prt1‐1 mutant, concomitant with increased accumulation of salicylic acid. The effects of the prt1 mutation were additional to known effects of prt6 in influencing the immune system, in particular, an observed over‐accumulation of pipecolic acid (Pip) in the double‐mutant prt1‐1 prt6‐1. These results demonstrate a potential role for PRT1 in controlling aspects of the plant immune system and suggest that PRT1 limits the onset of the defense response via degradation of substrates with type 2 Nt‐destabilizing residues. John Wiley and Sons Inc. 2019-12-26 /pmc/articles/PMC6933115/ /pubmed/31891113 http://dx.doi.org/10.1002/pld3.194 Text en © 2019 The Authors. Plant Direct published by American Society of Plant Biologists, Society for Experimental Biology and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Research
Till, Christopher J.
Vicente, Jorge
Zhang, Hongtao
Oszvald, Maria
Deery, Michael J.
Pastor, Victoria
Lilley, Kathryn S.
Ray, Rumiana V.
Theodoulou, Frederica L.
Holdsworth, Michael J.
The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response
title The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response
title_full The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response
title_fullStr The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response
title_full_unstemmed The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response
title_short The Arabidopsis thaliana N‐recognin E3 ligase PROTEOLYSIS1 influences the immune response
title_sort arabidopsis thaliana n‐recognin e3 ligase proteolysis1 influences the immune response
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6933115/
https://www.ncbi.nlm.nih.gov/pubmed/31891113
http://dx.doi.org/10.1002/pld3.194
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