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

International Journal of Molecular Sciences
Andrea PitzschkeGeorg J Seifert

Abstract

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 ...Continue Reading

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Citations

May 3, 2019·Plant, Cell & Environment·Christian DuttonJulie E Gray
May 30, 2019·International Journal of Molecular Sciences·Jinhua LiXingguo Zhang
Nov 30, 2018·BMC Microbiology·Sree Gowrinadh JavvadiVittorio Venturi
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Feb 3, 2019·Plant Science : an International Journal of Experimental Plant Biology·M B ShineAardra Kachroo

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Methods Mentioned

BETA
transgenic
glycosylation
transgenics
dot
dot blot
dot blots
protein extraction

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