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Plant Proteomics 2017

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A special issue of Proteomes (ISSN 2227-7382).

Deadline for manuscript submissions: closed (30 June 2017) | Viewed by 50918

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Dr. Véronique Santoni

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Guest Editor

Biochimie et Physiologie Moléculaire des Plantes, INRA/CNRS/SupAgro/UM2, UMR 5004, Montpellier CEDEX 1, France
Interests: aquaporin; phosphorylation; plant membrane; quantitative proteomics

Dr. Elisabeth Jamet

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Guest Editor

Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, CNRS, UPS, 24 Chemin de Borde Rouge, 31320 Auzeville-Tolosane, France
Interests: plant; cell wall biology; development; evolution; proteomics; post-translational modification; cell wall architecture; protein/protein; protein/polysaccharide interaction
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Special Issue Information

Dear Colleagues,

During recent years, proteomics has become the key to understand physiological processes involving the regulation of expression of many genes from transcription to production of metabolites. Each of these steps is part of the overall mechanisms tightly coordinated to allow organisms to develop or adapt to their environment. Plant proteomics has been dramatically expanding since the beginning of the 2000s thanks to major advances in the development of three technological tools. It started with the sequencing of full genomes and collection of expressed sequence tags or RNAs. The release of the Arabidopsis thaliana genome in 2000 has allowed this plant to become a pioneer model for dicots, and particularly for proteomics studies. More than 650 articles have been published in this field since 2000. A. thaliana has been quickly followed by Brachypodium distachyon as a model for monocots and by plants of agronomical interest such as rice, maize, sugarcane, alfalfa, tomato or flax. Apart from these plants, others for which sequencing data were not available could be studied as well, thanks to the possibility to work with heterologous data. In addition, over the last decade, remarkable technological advances have been achieved due to improvements in mass spectrometry which allowed refining the coverage of total proteomes and sub-proteomes from small amounts of starting material and characterizing post-translational modifications and protein-protein interactions. Furthermore, quantitative proteomics now provides detailed information on organ- and tissue-specific regulatory mechanisms responding to a variety of individual stresses or stress combinations during the plant life cycle. Finally, the development of computational tools allows managing the tremendous amount of data generated by mass spectrometers to deliver relevant biological information. Thus, powerful mass spectrometry-based technologies now provide unprecedented insights into the composition, structure, function and control of the proteome, shedding light on complex biological processes and phenotypes.

This Special issue of Proteomes welcomes submissions of original research or review articles aiming at deciphering physiological processes with the use of proteomics tools. Contributions will deal with the dynamics of proteins in their native and modified forms, with the combination of several “omics” approaches in contrasted physiological situations as well as with technical advances in the proteomic field.

Dr. Elisabeth Jamet
Dr. Véronique Santoni
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. Proteomes is an international peer-reviewed open access quarterly 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

Omics data integration
Plant development
Plant interactions with their environment
Plant proteomics
Quantitative proteomics

Published Papers (10 papers)

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Editorial

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3 pages, 168 KiB

Open AccessEditorial

Editorial for Special Issue: 2017 Plant Proteomics

by Elisabeth Jamet and Véronique Santoni

Proteomes 2018, 6(3), 28; https://doi.org/10.3390/proteomes6030028 - 21 Jun 2018

Cited by 3 | Viewed by 3215

Abstract

n/a Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

Research

Jump to: Editorial

34 pages, 2136 KiB

Open AccessArticle

Large Scale Proteomic Data and Network-Based Systems Biology Approaches to Explore the Plant World

by Dario Di Silvestre, Andrea Bergamaschi, Edoardo Bellini and PierLuigi Mauri

Proteomes 2018, 6(2), 27; https://doi.org/10.3390/proteomes6020027 - 03 Jun 2018

Cited by 15 | Viewed by 6472

Abstract

The investigation of plant organisms by means of data-derived systems biology approaches based on network modeling is mainly characterized by genomic data, while the potential of proteomics is largely unexplored. This delay is mainly caused by the paucity of plant genomic/proteomic sequences and annotations which are fundamental to perform mass-spectrometry (MS) data interpretation. However, Next Generation Sequencing (NGS) techniques are contributing to filling this gap and an increasing number of studies are focusing on plant proteome profiling and protein-protein interactions (PPIs) identification. Interesting results were obtained by evaluating the topology of PPI networks in the context of organ-associated biological processes as well as plant-pathogen relationships. These examples foreshadow well the benefits that these approaches may provide to plant research. Thus, in addition to providing an overview of the main-omic technologies recently used on plant organisms, we will focus on studies that rely on concepts of module, hub and shortest path, and how they can contribute to the plant discovery processes. In this scenario, we will also consider gene co-expression networks, and some examples of integration with metabolomic data and genome-wide association studies (GWAS) to select candidate genes will be mentioned. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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14 pages, 682 KiB

Open AccessArticle

Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass

by Mahesh Rangu, Zhujia Ye, Sarabjit Bhatti, Suping Zhou, Yong Yang, Tara Fish and Theodore W. Thannhauser

Proteomes 2018, 6(2), 15; https://doi.org/10.3390/proteomes6020015 - 22 Mar 2018

Cited by 6 | Viewed by 5023

Abstract

In this paper, we report on aluminum (Al)-induced root proteomic changes in switchgrass. After growth in a hydroponic culture system supplemented with 400 μM of Al, plants began to show signs of physiological stress such as a reduction in photosynthetic rate. At this time, the basal 2-cm long root tips were harvested and divided into two segments, each of 1-cm in length, for protein extraction. Al-induced changes in proteomes were identified using tandem mass tags mass spectrometry (TMT-MS)-based quantitative proteomics analysis. A total of 216 proteins (approximately 3.6% of total proteins) showed significant differences between non-Al treated control and treated groups with significant fold change (twice the standard deviation; FDR adjusted p-value < 0.05). The apical root tip tissues expressed more dramatic proteome changes (164 significantly changed proteins; 3.9% of total proteins quantified) compared to the elongation/maturation zones (52 significantly changed proteins, 1.1% of total proteins quantified). Significantly changed proteins from the apical 1-cm root apex tissues were clustered into 25 biological pathways; proteins involved in the cell cycle (rotamase FKBP 1 isoforms, and CDC48 protein) were all at a reduced abundance level compared to the non-treated control group. In the root elongation/maturation zone tissues, the identified proteins were placed into 18 pathways, among which proteins involved in secondary metabolism (lignin biosynthesis) were identified. Several STRING protein interaction networks were developed for these Al-induced significantly changed proteins. This study has identified a large number of Al-responsive proteins, including transcription factors, which will be used for exploring new Al tolerance genes and mechanisms. Data are available via ProteomeXchange with identifiers PXD008882 and PXD009125. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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23 pages, 4667 KiB

Open AccessFeature PaperArticle

The Secretome and N-Glycosylation Profiles of the Charophycean Green Alga, Penium margaritaceum, Resemble Those of Embryophytes

by Eliel Ruiz-May, Iben Sørensen, Zhangjun Fei, Sheng Zhang, David S. Domozych and Jocelyn K. C. Rose

Proteomes 2018, 6(2), 14; https://doi.org/10.3390/proteomes6020014 - 21 Mar 2018

Cited by 15 | Viewed by 5883

Abstract

The secretome can be defined as the population of proteins that are secreted into the extracellular environment. Many proteins that are secreted by eukaryotes are N-glycosylated. However, there are striking differences in the diversity and conservation of N-glycosylation patterns between taxa. For example, the secretome and N-glycosylation structures differ between land plants and chlorophyte green algae, but it is not clear when this divergence took place during plant evolution. A potentially valuable system to study this issue is provided by the charophycean green algae (CGA), which is the immediate ancestors of land plants. In this study, we used lectin affinity chromatography (LAC) coupled with mass spectrometry to characterize the secretome including secreted N-glycoproteins of Penium margaritaceum, which is a member of the CGA. The identified secreted proteins and N-glycans were compared to those known from the chlorophyte green alga Chlamydomonas reinhardtii and the model land plant, Arabidopsis thaliana, to establish their evolutionary context. Our approach allowed the identification of cell wall proteins and proteins modified with N-glycans that are identical to those of embryophytes, which suggests that the P. margaritaceum secretome is more closely related to those of land plants than to those of chlorophytes. The results of this study support the hypothesis that many of the proteins associated with plant cell wall modification as well as other extracellular processes evolved prior to the colonization of terrestrial habitats. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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14 pages, 2765 KiB

Open AccessFeature PaperArticle

Evaluation of Optimized Tube-Gel Methods of Sample Preparation for Large-Scale Plant Proteomics

by Thierry Balliau, Mélisande Blein-Nicolas and Michel Zivy

Proteomes 2018, 6(1), 6; https://doi.org/10.3390/proteomes6010006 - 30 Jan 2018

Cited by 16 | Viewed by 4241

Abstract

The so-called tube-gel method is a sample preparation protocol allowing for management of SDS for protein solubilization through in-gel protein trapping. Because of its simplicity, we assumed that once miniaturized, this method could become a standard for large scale experiments. We evaluated the performances of two variants of the miniaturized version of the tube-gel method based on different solubilization buffers (Tris-SDS or urea-SDS). To this end, we compared them to two other digestion methods: (i) liquid digestion after protein solubilization in the absence of SDS (liquid method) and (ii) filter-aided sample preparation (FASP). As large-scale experiments may require long term gel storage, we also examined to which extent gel aging affected the results of the proteomics analysis. We showed that both tube-gel and FASP methods extracted membrane proteins better than the liquid method, while the latter allowed the identification and quantification of a greater number of proteins. All methods were equivalent regarding quantitative stability. However, important differences were observed regarding post-translational modifications. In particular, methionine oxidation was higher with the tube-gel method than with the other methods. Based on these results, and considering time, simplicity, and cost aspects, we conclude that the miniaturized tube-gel method is suitable for sample preparation in the context of large-scale experiments. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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12095 KiB

Open AccessArticle

A Proteomic Approach to Investigate the Drought Response in the Orphan Crop Eragrostis tef

by Rizqah Kamies, Jill M. Farrant, Zerihun Tadele, Gina Cannarozzi and Mohammed Suhail Rafudeen

Proteomes 2017, 5(4), 32; https://doi.org/10.3390/proteomes5040032 - 15 Nov 2017

Cited by 17 | Viewed by 5616

Abstract

The orphan crop, Eragrostis tef, was subjected to controlled drought conditions to observe the physiological parameters and proteins changing in response to dehydration stress. Physiological measurements involving electrolyte leakage, chlorophyll fluorescence and ultra-structural analysis showed tef plants tolerated water loss to 50% relative water content (RWC) before adverse effects in leaf tissues were observed. Proteomic analysis using isobaric tag for relative and absolute quantification (iTRAQ) mass spectrometry and appropriate database searching enabled the detection of 5727 proteins, of which 211 proteins, including a number of spliced variants, were found to be differentially regulated with the imposed stress conditions. Validation of the iTRAQ dataset was done with selected stress-related proteins, fructose-bisphosphate aldolase (FBA) and the protective antioxidant proteins, monodehydroascorbate reductase (MDHAR) and peroxidase (POX). Western blot analyses confirmed protein presence and showed increased protein abundance levels during water deficit while enzymatic activity for FBA, MDHAR and POX increased at selected RWC points. Gene ontology (GO)-term enrichment and analysis revealed terms involved in biotic and abiotic stress response, signaling, transport, cellular homeostasis and pentose metabolic processes, to be enriched in tef upregulated proteins, while terms linked to reactive oxygen species (ROS)-producing processes under water-deficit, such as photosynthesis and associated light harvesting reactions, manganese transport and homeostasis, the synthesis of sugars and cell wall catabolism and modification, to be enriched in tef downregulated proteins. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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2703 KiB

Open AccessArticle

Proteomic Investigations of Proteases Involved in Cotyledon Senescence: A Model to Explore the Genotypic Variability of Proteolysis Machinery Associated with Nitrogen Remobilization Efficiency during the Leaf Senescence of Oilseed Rape

by Marine Poret, Balakumaran Chandrasekar, Renier A. L. Van der Hoorn, Laurent Coquet, Thierry Jouenne and Jean-Christophe Avice

Proteomes 2017, 5(4), 29; https://doi.org/10.3390/proteomes5040029 - 02 Nov 2017

Cited by 11 | Viewed by 3917

Abstract

Oilseed rape is characterized by a low nitrogen remobilization efficiency during leaf senescence, mainly due to a lack of proteolysis. Because cotyledons are subjected to senescence, it was hypothesized that contrasting protease activities between genotypes may be distinguishable early in the senescence of cotyledons. To verify this assumption, our goals were to (i) characterize protease activities in cotyledons between two genotypes with contrasting nitrogen remobilization efficiency (Ténor and Samouraï) under limiting or ample nitrate supply; and (ii) test the role of salicylic acid (SA) and abscisic acid (ABA) in proteolysis regulation. Protease activities were measured and identified by a proteomics approach combining activity-based protein profiling with LC-MS/MS. As in senescing leaves, chlorophyll and protein contents decrease in senescing cotyledons and are correlated with an increase in serine and cysteine protease activities. Two RD21-like and SAG-12 proteases previously associated with an efficient proteolysis in senescing leaves of Ténor are also detected in senescing cotyledons. The infiltration of ABA and SA provokes the induction of senescence and several cysteine and serine protease activities. The study of protease activities during the senescence of cotyledons seems to be a promising experimental model to investigate the regulation and genotypic variability of proteolysis associated with efficient N remobilization. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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600 KiB

Open AccessArticle

A Microsomal Proteomics View of H₂O₂- and ABA-Dependent Responses

by May Alqurashi, Ludivine Thomas, Chris Gehring and Claudius Marondedze

Proteomes 2017, 5(3), 22; https://doi.org/10.3390/proteomes5030022 - 18 Aug 2017

Cited by 10 | Viewed by 5527

Abstract

The plant hormone abscisic acid (ABA) modulates a number of plant developmental processes and responses to stress. In planta, ABA has been shown to induce reactive oxygen species (ROS) production through the action of plasma membrane-associated nicotinamide adenine dinucleotide phosphate (NADPH)-oxidases. Although quantitative proteomics studies have been performed to identify ABA- or hydrogen peroxide (H₂O₂)-dependent proteins, little is known about the ABA- and H₂O₂-dependent microsomal proteome changes. Here, we examined the effect of 50 µM of either H₂O₂ or ABA on the Arabidopsis microsomal proteome using tandem mass spectrometry and identified 86 specifically H₂O₂-dependent, and 52 specifically ABA-dependent proteins that are differentially expressed. We observed differential accumulation of proteins involved in the tricarboxylic acid (TCA) cycle notably in response to H₂O₂. Of these, aconitase 3 responded to both H₂O₂ and ABA. Additionally, over 30 proteins linked to RNA biology responded significantly to both treatments. Gene ontology categories such as ‘response to stress’ and ‘transport’ were enriched, suggesting that H₂O₂ or ABA directly and/or indirectly cause complex and partly overlapping cellular responses. Data are available via ProteomeXchange with identifier PXD006513. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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1976 KiB

Open AccessArticle

A Combination of Histological, Physiological, and Proteomic Approaches Shed Light on Seed Desiccation Tolerance of the Basal Angiosperm Amborella trichopoda

by Matthieu Villegente, Philippe Marmey, Claudette Job, Marc Galland, Gwendal Cueff, Béatrice Godin, Loïc Rajjou, Thierry Balliau, Michel Zivy, Bruno Fogliani, Valérie Sarramegna-Burtet and Dominique Job

Proteomes 2017, 5(3), 19; https://doi.org/10.3390/proteomes5030019 - 28 Jul 2017

Cited by 10 | Viewed by 5314

Abstract

Desiccation tolerance allows plant seeds to remain viable in a dry state for years and even centuries. To reveal potential evolutionary processes of this trait, we have conducted a shotgun proteomic analysis of isolated embryo and endosperm from mature seeds of Amborella trichopoda, an understory shrub endemic to New Caledonia that is considered to be the basal extant angiosperm. The present analysis led to the characterization of 415 and 69 proteins from the isolated embryo and endosperm tissues, respectively. The role of these proteins is discussed in terms of protein evolution and physiological properties of the rudimentary, underdeveloped, Amborella embryos, notably considering that the acquisition of desiccation tolerance corresponds to the final developmental stage of mature seeds possessing large embryos. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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1299 KiB

Open AccessArticle

Exogenous Auxin Elicits Changes in the Arabidopsis thaliana Root Proteome in a Time-Dependent Manner

by William O. Slade, W. Keith Ray, Sherry B. Hildreth, Brenda S. J. Winkel and Richard F. Helm

Proteomes 2017, 5(3), 16; https://doi.org/10.3390/proteomes5030016 - 10 Jul 2017

Cited by 7 | Viewed by 4707

Abstract

Auxin is involved in many aspects of root development and physiology, including the formation of lateral roots. Improving our understanding of how the auxin response is mediated at the protein level over time can aid in developing a more complete molecular framework of the process. This study evaluates the effects of exogenous auxin treatment on the Arabidopsis root proteome after exposure of young seedlings to auxin for 8, 12, and 24 h, a timeframe permitting the initiation and full maturation of individual lateral roots. Root protein extracts were processed to peptides, fractionated using off-line strong-cation exchange, and analyzed using ultra-performance liquid chromatography and data independent acquisition-based mass spectrometry. Protein abundances were then tabulated using label-free techniques and evaluated for significant changes. Approximately 2000 proteins were identified during the time course experiment, with the number of differences between the treated and control roots increasing over the 24 h time period, with more proteins found at higher abundance with exposure to auxin than at reduced abundance. Although the proteins identified and changing in levels at each time point represented similar biological processes, each time point represented a distinct snapshot of the response. Auxin coordinately regulates many physiological events in roots and does so by influencing the accumulation and loss of distinct proteins in a time-dependent manner. Data are available via ProteomeXchange with the identifier PXD001400. Full article

(This article belongs to the Special Issue Plant Proteomics 2017)

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