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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: closed (31 July 2024) | Viewed by 7288

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

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Published Papers (5 papers)

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Research

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16 pages, 2807 KiB  
Article
Treatments with Diquat Reveal the Relationship between Protein Phosphatases (PP2A) and Oxidative Stress during Mitosis in Arabidopsis thaliana Root Meristems
by Adrienn Kelemen, Tamás Garda, Zoltán Kónya, Ferenc Erdődi, László Ujlaky-Nagy, Gabriella Petra Juhász, Csongor Freytag, Márta M-Hamvas and Csaba Máthé
Plants 2024, 13(14), 1896; https://doi.org/10.3390/plants13141896 - 10 Jul 2024
Viewed by 1002
Abstract
Reversible protein phosphorylation regulates various cellular mechanisms in eukaryotes by altering the conformation, activity, localization, and stability of substrate proteins. In Arabidopsis thaliana root meristems, histone post-translational modifications are crucial for proper cell division, and they are also involved in oxidative stress signaling. [...] Read more.
Reversible protein phosphorylation regulates various cellular mechanisms in eukaryotes by altering the conformation, activity, localization, and stability of substrate proteins. In Arabidopsis thaliana root meristems, histone post-translational modifications are crucial for proper cell division, and they are also involved in oxidative stress signaling. To investigate the link between reactive oxygen species (ROS) and mitosis, we treated various Arabidopsis genotypes, including wild-types and mutants showing dysfunctional PP2A, with the ROS-inducing herbicide diquat (DQ). Studying the c3c4 double catalytic subunit mutant and fass regulatory subunit mutants of PP2A provided insights into phosphorylation-dependent mitotic processes. DQ treatment reduced mitotic activity in all genotypes and caused early mitotic arrest in PP2A mutants, likely due to oxidative stress-induced damage to essential mitotic processes. DQ had a minimal effect on reversible histone H3 phosphorylation in wild-type plants but significantly decreased phospho-histone H3 levels in PP2A mutants. Following drug treatment, the phosphatase activity decreased only in the stronger phenotype mutant plants (fass-5 and c3c4). Our findings demonstrate that (i) the studied PP2A loss-of-function mutants are more sensitive to increased intracellular ROS and (ii) DQ has indirect altering effects of mitotic activities and histone H3 phosphorylation. All these findings underscore the importance of PP2A in stress responses. Full article
(This article belongs to the Special Issue Post-Translational Modifications in Plants)
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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
Cited by 1 | Viewed by 1418
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 ensues 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 1076
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 3 | Viewed by 1916
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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Review

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14 pages, 996 KiB  
Review
Post-Translational Modification of WRKY Transcription Factors
by Xiangui Zhou, Zaojuan Lei and Pengtian An
Plants 2024, 13(15), 2040; https://doi.org/10.3390/plants13152040 - 25 Jul 2024
Viewed by 813
Abstract
Post-translational modifications (PTMs) of proteins are involved in numerous biological processes, including signal transduction, cell cycle regulation, growth and development, and stress responses. WRKY transcription factors (TFs) play significant roles in plant growth, development, and responses to both biotic and abiotic stresses, making [...] Read more.
Post-translational modifications (PTMs) of proteins are involved in numerous biological processes, including signal transduction, cell cycle regulation, growth and development, and stress responses. WRKY transcription factors (TFs) play significant roles in plant growth, development, and responses to both biotic and abiotic stresses, making them one of the largest and most vital TF families in plants. Recent studies have increasingly highlighted the importance of PTMs of WRKY TFs in various life processes. This review focuses on the recent advancements in understanding the phosphorylation and ubiquitination of WRKY TFs, particularly their roles in resistance to biotic and abiotic stresses and in plant growth and development. Future research directions and prospects in this field are also discussed. Full article
(This article belongs to the Special Issue Post-Translational Modifications in Plants)
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