Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
5.4
4.5
Journals
Plants
Special Issues
Post-Translational Mechanisms Implicated in Stress-Related Responses and Plant-Pathogen Interactions
share announcement

Post-Translational Mechanisms Implicated in Stress-Related Responses and Plant-Pathogen Interactions

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Protection and Biotic Interactions".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 2197

Special Issue Editors

Dr. Amr Kataya

E-Mail Website
Guest Editor
Department of Biological Sciences, University of Calgary, Calgary, AB T2N 1N4, Canada
Interests: post-translational modifications; peroxisomal phospho-regulation; organelle crosstalk; organelle responses to stress; plant–pathogen interaction
Dr. Eric Fedosejevs

E-Mail Website
Co-Guest Editor
Department of Biochemistry, University of Missouri, 1201 E Rollins, Columbia, MO 65211, USA
Interests: post-translational modifications; glycosylation; protein kinases; sugar metabolism

Special Issue Information

Dear Colleagues,

When under stress and pathogen attack, the cell is performing a diverse and complex response, along with a multitude of other functions, including defined roles for cell organelles. Therefore, tight regulatory mechanisms are expected to fine-tune the ability of the cell and cell organelles to adapt to external stimuli, which requires highly dynamic and versatile processes, such as post-translational modifications (PTMs). PTMs are important for regulating gene expression and enzyme kinetics while maintaining protein stability and interactions and organelles crosstalk. Multiple types of PTMs, such as phosphorylation, ubiquitination, acetylation, and asparagine (N)-linked glycosylation, are anticipated to regulate plant metabolic enzymes and pathways. Reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-induced PTMs are also expected to be high in frequency under stress responses, especially in cell organelles, such as chloroplasts, mitochondria, and peroxisomes. Identifying these factors and their mechanistic regulation of the cell and cell organelles under biotic and abiotic stresses and during plant–pathogen interaction will offer new insights into basic sciences, as well as supplying useful approaches for adapting plants to environmental stresses by genetic engineering. This Special Issue of Plants will highlight PTMs and their mechanistic regulation in the plant cell organelles under stress-related responses and plant–pathogen interaction.

Dr. Amr Kataya
Dr. Eric Fedosejevs
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Plants is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (2 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

19 pages, 4010 KiB  
Article
Methyl-Jasmonate Functions as a Molecular Switch Promoting Cross-Talk between Pathways for the Biosynthesis of Isoprenoid Backbones Used to Modify Proteins in Plants
by Quentin Chevalier, Alexandre Huchelmann, Pauline Debié, Pierre Mercier, Michael Hartmann, Catherine Vonthron-Sénécheau, Thomas J. Bach, Hubert Schaller and Andréa Hemmerlin
Plants 2024, 13(8), 1110; https://doi.org/10.3390/plants13081110 - 16 Apr 2024
Viewed by 503
Abstract
In plants, the plastidial mevalonate (MVA)-independent pathway is required for the modification with geranylgeranyl groups of CaaL-motif proteins, which are substrates of protein geranylgeranyltransferase type-I (PGGT-I). As a consequence, fosmidomycin, a specific inhibitor of 1-deoxy-d-xylulose (DX)-5 phosphate reductoisomerase/DXR, the second enzyme [...] Read more.
In plants, the plastidial mevalonate (MVA)-independent pathway is required for the modification with geranylgeranyl groups of CaaL-motif proteins, which are substrates of protein geranylgeranyltransferase type-I (PGGT-I). As a consequence, fosmidomycin, a specific inhibitor of 1-deoxy-d-xylulose (DX)-5 phosphate reductoisomerase/DXR, the second enzyme in this so-called methylerythritol phosphate (MEP) pathway, also acts as an effective inhibitor of protein prenylation. This can be visualized in plant cells by confocal microscopy by expressing GFP-CaM-CVIL, a prenylation sensor protein. After treatment with fosmidomycin, the plasma membrane localization of this GFP-based sensor is altered, and a nuclear distribution of fluorescence is observed instead. In tobacco cells, a visual screen of conditions allowing membrane localization in the presence of fosmidomycin identified jasmonic acid methyl esther (MeJA) as a chemical capable of gradually overcoming inhibition. Using Arabidopsis protein prenyltransferase loss-of-function mutant lines expressing GFP-CaM-CVIL proteins, we demonstrated that in the presence of MeJA, protein farnesyltransferase (PFT) can modify the GFP-CaM-CVIL sensor, a substrate the enzyme does not recognize under standard conditions. Similar to MeJA, farnesol and MVA also alter the protein substrate specificity of PFT, whereas DX and geranylgeraniol have limited or no effect. Our data suggest that MeJA adjusts the protein substrate specificity of PFT by promoting a metabolic cross-talk directing the origin of the prenyl group used to modify the protein. MVA, or an MVA-derived metabolite, appears to be a key metabolic intermediate for this change in substrate specificity. Full article
(This article belongs to the Special Issue Post-Translational Mechanisms Implicated in Stress-Related Responses and Plant-Pathogen Interactions)
►▼ Show Figures

Figure 1

12 pages, 1719 KiB  
Article
Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme
by Ahmed Elshobaky, Cathrine Lillo, Kristian Persson Hodén and Amr R. A. Kataya
Plants 2023, 12(13), 2586; https://doi.org/10.3390/plants12132586 - 7 Jul 2023
Viewed by 1288
Abstract
Protein phosphatase 2A (PP2A) is a heterotrimeric conserved serine/threonine phosphatase complex that includes catalytic, scaffolding, and regulatory subunits. The 3 A subunits, 17 B subunits, and 5 C subunits that are encoded by the Arabidopsis genome allow 255 possible PP2A holoenzyme combinations. The [...] Read more.
Protein phosphatase 2A (PP2A) is a heterotrimeric conserved serine/threonine phosphatase complex that includes catalytic, scaffolding, and regulatory subunits. The 3 A subunits, 17 B subunits, and 5 C subunits that are encoded by the Arabidopsis genome allow 255 possible PP2A holoenzyme combinations. The regulatory subunits are crucial for substrate specificity and PP2A complex localization and are classified into the B, B’, and B” non-related families in land plants. In Arabidopsis, the close homologs B’η, B’θ, B’γ, and B’ζ are further classified into a subfamily of B’ called B’η. Previous studies have suggested that mitochondrial targeted PP2A subunits (B’ζ) play a role in energy metabolism and plant innate immunity. Potentially, the PP2A-B’ζ holoenzyme is involved in the regulation of the mitochondrial succinate/fumarate translocator, and it may affect the enzymes involved in energy metabolism. To investigate this hypothesis, the interactions between PP2A-B’ζ and the enzymes involved in the mitochondrial energy flow were investigated using bimolecular fluorescence complementation in tobacco and onion cells. Interactions were confirmed between the B’ζ subunit and the Krebs cycle proteins succinate/fumarate translocator (mSFC1), malate dehydrogenase (mMDH2), and aconitase (ACO3). Additional putative interacting candidates were deduced by comparing the enriched phosphoproteomes of wild type and B’ζ mutants: the mitochondrial regulator Arabidopsis pentatricopeptide repeat 6 (PPR6) and the two metabolic enzymes phosphoenolpyruvate carboxylase (PPC3) and phosphoenolpyruvate carboxykinase (PCK1). Overall, this study identifies potential PP2A substrates and highlights the role of PP2A in regulating energy metabolism in mitochondria. Full article
(This article belongs to the Special Issue Post-Translational Mechanisms Implicated in Stress-Related Responses and Plant-Pathogen Interactions)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-2
Back to TopTop