Post-Translational Modifications in Plants
A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Molecular Biology".
Deadline for manuscript submissions: 31 July 2024 | Viewed by 3993
Special Issue Editors
Interests: PEPC; PEPC kinase; salinity; post-translational modification; autophagy; nitric oxide; ubiquitin; phosphorylation; oxylipins; signaling
Interests: post-translational modifications (PTMs); plant nutrition; molecular plant biology; abiotic stress; nitric oxide; ubiquitin; phosphorylation; circadian clock; plant–microbe interactions
Interests: plant protein phosphorylation and carbon metabolism; the regulation of phosphoenolpyruvate carboxylase (PEPC) by post-translational modifications (phosphorylation and monoubiquitination); sorghum seeds
Special Issue Information
Dear Colleagues,
The post-translational modification (PTM) of plant proteins is an important process modulating enzymatic activity, protein stability, subcellular localization, and interaction with other molecules. Plant PTMs include reversible phosphorylation, ubiquitination, persulfidation, S-nitrosylation, acetylation, SUMOylation, glycosylation, lipidation, and carbonylation, among others. Many of them are central modules in signal transduction controlling plant growth and development as well as responses to environmental stresses. Recent advances in biochemistry and molecular biology are helping us to reach an unprecedented understanding of PTMs in plants. This Special Issue of Plants will highlight the function of PTM and its significance in biotic and abiotic stress as well as hormonal signaling. In addition, insights into proteome are also welcome.
Dr. Sofía García-Mauriño
Dr. José Antonio Monreal
Dr. Ana Belén Feria
Guest Editors
Manuscript Submission Information
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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.
Keywords
- calcium-dependent protein kinases
- kinase gene family
- kinome
- mitogen-activated protein kinase
- phosphorylation
- phosphorylome
- plant protein kinase
- protein turnover
- stress signaling
- hormonal signaling
- sucrose non-fermenting 1 (SNF1)-related protein kinase
- phosphatases
- ubiquitin
- ubiquitination
- ubiquitinome
- reactive nitrogen species (RNS)
- reactive oxygen species (ROS)
- acetylation
- lipidation
- farnesylation
- myristoylation
- carbonylation
- sumoylation
- glycosylation
Planned Papers
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Treatments with diquat reveal the relationship between protein phosphatases (PP2A) and reactive oxygen species (ROS) during mitosis in Arabidopsis thaliana root meristems
Authors: Adrienn Kelemen; Tamás Garda; Zoltán Kónya; Ferenc Erdődi; Gabriella Petra Juhász; Csongor Freytag; Csaba Máthé
Affiliation: 1.) Department of Botany, Faculty of Science and Technology, University of Debrecen, H-4032 Debrecen, Hungary 2.) Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary
Abstract: Reversible protein phosphorylation regulates various cellular mechanisms in eukaryotic cells by modulating the conformation, activity, localization, and stability of substrate proteins. Histones are the main components of chromatin and are regulated by many post-translational modifications. For the proper cell division in Arabidopsis thaliana root meristems, reversible phosphorylation of histone H3 is required and involved mainly in chromosome segregation. Oxidative stress signaling pathways often involve these post-translational modification mechanisms as well. ROS-inducing herbicide (diquat, DQ) treatment were used to examine the correlation between reactive oxygen species and mitosis. We studied various Arabidopsis genotypes, including wild type and mutants impaired in PP2A activity. Examining protein phosphatase mutants (c3c4 double catalytic subunit mutant and fass regulatory subunit mutant plants) will provide a better insight into the more precise mechanisms of phosphorylation-dependent mitotic processes. The drug had a minimal impact on reversible histone H3 phosphorylation in wild-type plants compared to mutants, where PP2A was inhibited. In the phosphatase mutants, diquat treatment induced different changes in phosphorylation levels during mitosis; both increased and decreased phosphorylation state can be observed. Following drug treatment, the phosphatase activity decreased only in c3c4 mutants as compared to the other genotypes, which can show us that the catalytic subunit was affected by oxidative stress. The herbicide significantly reduced the mitotic activity across all genotypes at different concentration levels. The reduction in mitotic activity in plants after diquat treatment is likely a consequence of oxidative stress-induced damage to cellular processes essential for proper mitotic progression. By examining protein phosphatase mutant plants and inducing oxidative stress, we are able to study the relationships between phosphorylation dependent processes and the mechanism of stress responses under different concentrations of drug/herbicide treatments.