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Post-Translational Modifications in Plants
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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 3850

Special Issue Editors

Dr. Sofía García-Mauriño

E-Mail Website
Guest Editor
Department of Plant Biology and Ecology, Faculty of Biology, University of Seville, 41012 Seville, Spain
Interests: PEPC; PEPC kinase; salinity; post-translational modification; autophagy; nitric oxide; ubiquitin; phosphorylation; oxylipins; signaling
Dr. José Antonio Monreal

E-Mail Website
Guest Editor
Department of Plant Biology and Ecology, Faculty of Biology, University of Seville, 41012 Seville, Spain
Interests: post-translational modifications (PTMs); plant nutrition; molecular plant biology; abiotic stress; nitric oxide; ubiquitin; phosphorylation; circadian clock; plant–microbe interactions
Dr. Ana Belén Feria

E-Mail Website
Guest Editor
Department of Plant Biology and Ecology, Faculty of Biology, University of Seville, 41012 Seville, Spain
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

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.

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

Published Papers (3 papers)

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Research

18 pages, 3439 KiB  
Article
In Vivo Phosphorylation of the Cytosolic Glucose-6-Phosphate Dehydrogenase Isozyme G6PD6 in Phosphate-Resupplied Arabidopsis thaliana Suspension Cells and Seedlings
by Milena A. Smith, Kirsten H. Benidickson and William C. Plaxton
Plants 2024, 13(1), 31; https://doi.org/10.3390/plants13010031 - 21 Dec 2023
Viewed by 859
Abstract
Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the first committed step of the oxidative pentose phosphate pathway (OPPP). Our recent phosphoproteomics study revealed that the cytosolic G6PD6 isozyme became hyperphosphorylated at Ser12, Thr13 and Ser18, 48 h following phosphate (Pi) resupply to Pi-starved (–Pi) Arabidopsis thaliana [...] Read more.
Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the first committed step of the oxidative pentose phosphate pathway (OPPP). Our recent phosphoproteomics study revealed that the cytosolic G6PD6 isozyme became hyperphosphorylated at Ser12, Thr13 and Ser18, 48 h following phosphate (Pi) resupply to Pi-starved (–Pi) Arabidopsis thaliana cell cultures. The aim of the present study was to assess whether G6PD6 phosphorylation also occurs in shoots or roots following Pi resupply to –Pi Arabidopsis seedlings, and to investigate its relationship with G6PD activity. Interrogation of phosphoproteomic databases indicated that N-terminal, multi-site phosphorylation of G6PD6 and its orthologs is quite prevalent. However, the functions of these phosphorylation events remain unknown. Immunoblotting with an anti-(pSer18 phosphosite-specific G6PD6) antibody confirmed that G6PD6 from Pi-resupplied, but not –Pi, Arabidopsis cell cultures or seedlings (i.e., roots) was phosphorylated at Ser18; this correlated with a significant increase in extractable G6PD activity, and biomass accumulation. Peptide kinase assays of Pi-resupplied cell culture extracts indicated that G6PD6 phosphorylation at Ser18 is catalyzed by a Ca2+-dependent protein kinase (CDPK), which correlates with the ‘CDPK-like’ targeting motif that flanks Ser18. Our results support the hypothesis that N-terminal phosphorylation activates G6PD6 to enhance OPPP flux and thus the production of reducing power (i.e., NADPH) and C-skeletons needed to establish the rapid resumption of growth that ensures Pi-resupply to –Pi Arabidopsis. Full article
(This article belongs to the Special Issue Post-Translational Modifications in Plants)
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20 pages, 1813 KiB  
Article
Silencing of SbPPCK1-3 Negatively Affects Development, Stress Responses and Productivity in Sorghum
by Jesús Pérez-López, Ana B. Feria, Jacinto Gandullo, Clara de la Osa, Irene Jiménez-Guerrero, Cristina Echevarría, José A. Monreal and Sofía García-Mauriño
Plants 2023, 12(13), 2426; https://doi.org/10.3390/plants12132426 - 23 Jun 2023
Viewed by 767
Abstract
Phosphoenolpyruvate carboxylase (PEPC) plays central roles in photosynthesis, respiration, amino acid synthesis, and seed development. PEPC is regulated by different post-translational modifications. Between them, the phosphorylation by PEPC-kinase (PEPCk) is widely documented. In this work, we simultaneously silenced the three sorghum genes encoding [...] Read more.
Phosphoenolpyruvate carboxylase (PEPC) plays central roles in photosynthesis, respiration, amino acid synthesis, and seed development. PEPC is regulated by different post-translational modifications. Between them, the phosphorylation by PEPC-kinase (PEPCk) is widely documented. In this work, we simultaneously silenced the three sorghum genes encoding PEPCk (SbPPCK1-3) by RNAi interference, obtaining 12 independent transgenic lines (Ppck1-12 lines), showing different degrees of SbPPCK1-3 silencing. Among them, two T2 homozygous lines (Ppck-2 and Ppck-4) were selected for further evaluation. Expression of SbPPCK1 was reduced by 65% and 83% in Ppck-2 and Ppck-4 illuminated leaves, respectively. Expression of SbPPCK2 was higher in roots and decreased by 50% in Ppck-2 and Ppck-4 in this tissue. Expression of SbPPCK3 was low and highly variable. Despite the incomplete gene silencing, it decreased the degree of phosphorylation of PEPC in illuminated leaves, P-deficient plants, and NaCl-treated plants. Both leaves and seeds of Ppck lines had altered metabolic profiles and a general decrease in amino acid content. In addition, Ppck lines showed delayed flowering, and 20% of Ppck-4 plants did not produce flowers at all. The total amount of seeds was lowered by 50% and 36% in Ppck-2 and Ppck-4 lines, respectively. The quality of seeds was lower in Ppck lines: lower amino acid content, including Lys, and higher phytate content. These data confirm the relevance of the phosphorylation of PEPC in sorghum development, stress responses, yield, and quality of seeds. Full article
(This article belongs to the Special Issue Post-Translational Modifications in Plants)
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19 pages, 1942 KiB  
Article
Receptor for Activated C Kinase1B (RACK1B) Delays Salinity-Induced Senescence in Rice Leaves by Regulating Chlorophyll Degradation
by Md Ahasanur Rahman and Hemayet Ullah
Plants 2023, 12(12), 2385; https://doi.org/10.3390/plants12122385 - 20 Jun 2023
Cited by 2 | Viewed by 1519
Abstract
The widely conserved Receptor for Activated C Kinase1 (RACK1) protein is a WD-40 type scaffold protein that regulates diverse environmental stress signal transduction pathways. Arabidopsis RACK1A has been reported to interact with various proteins in salt stress and Light-Harvesting Complex (LHC) pathways. However, [...] Read more.
The widely conserved Receptor for Activated C Kinase1 (RACK1) protein is a WD-40 type scaffold protein that regulates diverse environmental stress signal transduction pathways. Arabidopsis RACK1A has been reported to interact with various proteins in salt stress and Light-Harvesting Complex (LHC) pathways. However, the mechanism of how RACK1 contributes to the photosystem and chlorophyll metabolism in stress conditions remains elusive. In this study, using T-DNA-mediated activation tagging transgenic rice (Oryza sativa L.) lines, we show that leaves from rice RACK1B gene (OsRACK1B) gain-of-function (RACK1B-OX) plants exhibit the stay-green phenotype under salinity stress. In contrast, leaves from down-regulated OsRACK1B (RACK1B-UX) plants display an accelerated yellowing. qRT-PCR analysis revealed that several genes which encode chlorophyll catabolic enzymes (CCEs) are differentially expressed in both RACK1B-OX and RACK1B-UX rice plants. In addition to CCEs, stay-green (SGR) is a key component that forms the SGR-CCE complex in senescing chloroplasts, and which causes LHCII complex instability. Transcript and protein profiling revealed a significant upregulation of OsSGR in RACK1B-UX plants compared to that in RACK1B-OX rice plants during salt treatment. The results imply that senescence-associated transcription factors (TFs) are altered following altered OsRACK1B expression, indicating a transcriptional reprogramming by OsRACK1B and a novel regulatory mechanism involving the OsRACK1B-OsSGR-TFs complex. Our findings suggest that the ectopic expression of OsRACK1B negatively regulates chlorophyll degradation, leads to a steady level of LHC-II isoform Lhcb1, an essential prerequisite for the state transition of photosynthesis for adaptation, and delays salinity-induced senescence. Taken together, these results provide important insights into the molecular mechanisms of salinity-induced senescence, which can be useful in circumventing the effect of salt on photosynthesis and in reducing the yield penalty of important cereal crops, such as rice, in global climate change conditions. Full article
(This article belongs to the Special Issue Post-Translational Modifications in Plants)
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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.

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