Cargando…

Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis

Arabidopsis EARLI-type hybrid proline-rich proteins (HyPRPs) consist of a putative N-terminal secretion signal, a proline-rich domain (PRD), and a characteristic eight-cysteine-motif (8-CM). They have been implicated in biotic and abiotic stress responses. AZI1 is required for systemic acquired resi...

Descripción completa

Detalles Bibliográficos
Autores principales: Pitzschke, Andrea, Xue, Hui, Persak, Helene, Datta, Sneha, Seifert, Georg J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730328/
https://www.ncbi.nlm.nih.gov/pubmed/26771603
http://dx.doi.org/10.3390/ijms17010085
_version_ 1782412377363316736
author Pitzschke, Andrea
Xue, Hui
Persak, Helene
Datta, Sneha
Seifert, Georg J.
author_facet Pitzschke, Andrea
Xue, Hui
Persak, Helene
Datta, Sneha
Seifert, Georg J.
author_sort Pitzschke, Andrea
collection PubMed
description Arabidopsis EARLI-type hybrid proline-rich proteins (HyPRPs) consist of a putative N-terminal secretion signal, a proline-rich domain (PRD), and a characteristic eight-cysteine-motif (8-CM). They have been implicated in biotic and abiotic stress responses. AZI1 is required for systemic acquired resistance and it has recently been identified as a target of the stress-induced mitogen-activated protein kinase MPK3. AZI1 gel migration properties strongly indicate AZI1 to undergo major post-translational modifications. These occur in a stress-independent manner and are unrelated to phosphorylation by MAPKs. As revealed by transient expression of AZI1 in Nicotiana benthamiana and Tropaeolum majus, the Arabidopsis protein is similarly modified in heterologous plant species. Proline-rich regions, resembling arabinogalactan proteins point to a possible proline hydroxylation and subsequent O-glycosylation of AZI1. Consistently, inhibition of prolyl hydroxylase reduces its apparent protein size. AZI1 secretion was examined using Arabidopsis protoplasts and seedling exudates. Employing Agrobacterium-mediated leaf infiltration of N. benthamiana, we attempted to assess long-distance movement of AZI1. In summary, the data point to AZI1 being a partially secreted protein and a likely new member of the group of hydroxyproline-rich glycoproteins. Its dual location suggests AZI1 to exert both intra- and extracellular functions.
format Online
Article
Text
id pubmed-4730328
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-47303282016-02-11 Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis Pitzschke, Andrea Xue, Hui Persak, Helene Datta, Sneha Seifert, Georg J. Int J Mol Sci Article Arabidopsis EARLI-type hybrid proline-rich proteins (HyPRPs) consist of a putative N-terminal secretion signal, a proline-rich domain (PRD), and a characteristic eight-cysteine-motif (8-CM). They have been implicated in biotic and abiotic stress responses. AZI1 is required for systemic acquired resistance and it has recently been identified as a target of the stress-induced mitogen-activated protein kinase MPK3. AZI1 gel migration properties strongly indicate AZI1 to undergo major post-translational modifications. These occur in a stress-independent manner and are unrelated to phosphorylation by MAPKs. As revealed by transient expression of AZI1 in Nicotiana benthamiana and Tropaeolum majus, the Arabidopsis protein is similarly modified in heterologous plant species. Proline-rich regions, resembling arabinogalactan proteins point to a possible proline hydroxylation and subsequent O-glycosylation of AZI1. Consistently, inhibition of prolyl hydroxylase reduces its apparent protein size. AZI1 secretion was examined using Arabidopsis protoplasts and seedling exudates. Employing Agrobacterium-mediated leaf infiltration of N. benthamiana, we attempted to assess long-distance movement of AZI1. In summary, the data point to AZI1 being a partially secreted protein and a likely new member of the group of hydroxyproline-rich glycoproteins. Its dual location suggests AZI1 to exert both intra- and extracellular functions. MDPI 2016-01-12 /pmc/articles/PMC4730328/ /pubmed/26771603 http://dx.doi.org/10.3390/ijms17010085 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Pitzschke, Andrea
Xue, Hui
Persak, Helene
Datta, Sneha
Seifert, Georg J.
Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis
title Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis
title_full Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis
title_fullStr Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis
title_full_unstemmed Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis
title_short Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis
title_sort post-translational modification and secretion of azelaic acid induced 1 (azi1), a hybrid proline-rich protein from arabidopsis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730328/
https://www.ncbi.nlm.nih.gov/pubmed/26771603
http://dx.doi.org/10.3390/ijms17010085
work_keys_str_mv AT pitzschkeandrea posttranslationalmodificationandsecretionofazelaicacidinduced1azi1ahybridprolinerichproteinfromarabidopsis
AT xuehui posttranslationalmodificationandsecretionofazelaicacidinduced1azi1ahybridprolinerichproteinfromarabidopsis
AT persakhelene posttranslationalmodificationandsecretionofazelaicacidinduced1azi1ahybridprolinerichproteinfromarabidopsis
AT dattasneha posttranslationalmodificationandsecretionofazelaicacidinduced1azi1ahybridprolinerichproteinfromarabidopsis
AT seifertgeorgj posttranslationalmodificationandsecretionofazelaicacidinduced1azi1ahybridprolinerichproteinfromarabidopsis