Special Issue "Plant Proteostasis"

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

Deadline for manuscript submissions: 31 January 2020.

Special Issue Editor

Guest Editor
Dr. Panagiotis Nikolaou Moschou

Researcher (Associate Professor) in Molecular and Cellular Biology, The Swedish University of Agricultural Sciences
Website | E-Mail
Phone: +46-018-673315
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

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 papers will be 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 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 1200 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 (1 paper)

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Research

Open AccessArticle
Role of ClpP in the Biogenesis and Degradation of RuBisCO and ATP Synthase in Chlamydomonas reinhardtii
Received: 23 May 2019 / Revised: 17 June 2019 / Accepted: 19 June 2019 / Published: 26 June 2019
PDF Full-text (6167 KB) | HTML Full-text | XML Full-text | Supplementary Files
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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