Special Issue "Plant Proteostasis"

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Molecular Biology".

Deadline for manuscript submissions: closed (31 January 2020).

Special Issue Editor

Dr. Panagiotis Nikolaou Moschou
E-Mail Website
Guest Editor
Researcher (Associate Professor) in Molecular and Cellular Biology, The Swedish University of Agricultural Sciences
Interests: plant catabolic processes; proteostasis; RNA turnover; plant biotechnology

Special Issue Information

Dear Colleagues,

Proteostasis is regulated, among others, by proteolytic degradation through bulk proteolytic machineries (proteasome and autophagy), but also by a diverse and fascinating group of proteases that execute limited proteolysis. Exploiting the chemical diversity and functions of proteolytic pathways could generate new leads for improving plants and related biobased products. Much remains to be discovered, as we now have new methods for determining the fate and turnover of proteins, important proteases, and their corresponding substrates. Furthermore, proteolytic degradation pathway engineering is now expanding from models to crops, with the potential to benefit productivity and environmental resilience to threats. This Special Issue of Plants will highlight the molecular aspects, evolution, and diversity of plant proteostasis.

Dr. Panagiotis Nikolaou Moschou
Guest Editor

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 monthly 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 1800 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

  • proteases
  • proteasome
  • autophagy
  • proteostasis
  • ubiquitin
  • proteomics

Published Papers (2 papers)

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Research

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Article
Role of ClpP in the Biogenesis and Degradation of RuBisCO and ATP Synthase in Chlamydomonas reinhardtii
Plants 2019, 8(7), 191; https://doi.org/10.3390/plants8070191 - 26 Jun 2019
Cited by 2 | Viewed by 1519
Abstract
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) associates a chloroplast- and a nucleus-encoded subunit (LSU and SSU). It constitutes the major entry point of inorganic carbon into the biosphere as it catalyzes photosynthetic CO2 fixation. Its abundance and richness in sulfur-containing amino acids make it [...] Read more.
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) associates a chloroplast- and a nucleus-encoded subunit (LSU and SSU). It constitutes the major entry point of inorganic carbon into the biosphere as it catalyzes photosynthetic CO2 fixation. Its abundance and richness in sulfur-containing amino acids make it a prime source of N and S during nutrient starvation, when photosynthesis is downregulated and a high RuBisCO level is no longer needed. Here we show that translational attenuation of ClpP1 in the green alga Chlamydomonas reinhardtii results in retarded degradation of RuBisCO during S- and N-starvation, suggesting that the Clp protease is a major effector of RubisCO degradation in these conditions. Furthermore, we show that ClpP cannot be attenuated in the context of rbcL point mutations that prevent LSU folding. The mutant LSU remains in interaction with the chloroplast chaperonin complex. We propose that degradation of the mutant LSU by the Clp protease is necessary to prevent poisoning of the chaperonin. In the total absence of LSU, attenuation of ClpP leads to a dramatic stabilization of unassembled SSU, indicating that Clp is responsible for its degradation. In contrast, attenuation of ClpP in the absence of SSU does not lead to overaccumulation of LSU, whose translation is controlled by assembly. Altogether, these results point to RuBisCO degradation as one of the major house-keeping functions of the essential Clp protease. In addition, we show that non-assembled subunits of the ATP synthase are also stabilized when ClpP is attenuated. In the case of the atpA-FUD16 mutation, this can even allow the assembly of a small amount of CF1, which partially restores phototrophy. Full article
(This article belongs to the Special Issue Plant Proteostasis)
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Review

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Review
The Role of Proteases in Determining Stomatal Development and Tuning Pore Aperture: A Review
Plants 2020, 9(3), 340; https://doi.org/10.3390/plants9030340 - 08 Mar 2020
Cited by 11 | Viewed by 1694
Abstract
Plant proteases, the proteolytic enzymes that catalyze protein breakdown and recycling, play an essential role in a variety of biological processes including stomatal development and distribution, as well as, systemic stress responses. In this review, we summarize what is known about the participation [...] Read more.
Plant proteases, the proteolytic enzymes that catalyze protein breakdown and recycling, play an essential role in a variety of biological processes including stomatal development and distribution, as well as, systemic stress responses. In this review, we summarize what is known about the participation of proteases in both stomatal organogenesis and on the stomatal pore aperture tuning, with particular emphasis on their involvement in numerous signaling pathways triggered by abiotic and biotic stressors. There is a compelling body of evidence demonstrating that several proteases are directly or indirectly implicated in the process of stomatal development, affecting stomatal index, density, spacing, as well as, size. In addition, proteases are reported to be involved in a transient adjustment of stomatal aperture, thus orchestrating gas exchange. Consequently, the proteases-mediated regulation of stomatal movements considerably affects plants’ ability to cope not only with abiotic stressors, but also to perceive and respond to biotic stimuli. Even though the determining role of proteases on stomatal development and functioning is just beginning to unfold, our understanding of the underlying processes and cellular mechanisms still remains far from being completed. Full article
(This article belongs to the Special Issue Plant Proteostasis)
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