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

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          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.

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          Seed germination and vigor.

          Loïc Rajjou, Manuel Duval, Karine Gallardo … (2012)
          Germination vigor is driven by the ability of the plant embryo, embedded within the seed, to resume its metabolic activity in a coordinated and sequential manner. Studies using "-omics" approaches support the finding that a main contributor of seed germination success is the quality of the messenger RNAs stored during embryo maturation on the mother plant. In addition, proteostasis and DNA integrity play a major role in the germination phenotype. Because of its pivotal role in cell metabolism and its close relationships with hormone signaling pathways regulating seed germination, the sulfur amino acid metabolism pathway represents a key biochemical determinant of the commitment of the seed to initiate its development toward germination. This review highlights that germination vigor depends on multiple biochemical and molecular variables. Their characterization is expected to deliver new markers of seed quality that can be used in breeding programs and/or in biotechnological approaches to improve crop yields.
          Article 0 comments Cited 295 times – based on 0 reviews     Review now
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            The heat‐shock protein/chaperone network and multiple stress resistance

            Pierre Jacob, Heribert Hirt, Abdelhafid Bendahmane (2017)
            Summary Crop yield has been greatly enhanced during the last century. However, most elite cultivars are adapted to temperate climates and are not well suited to more stressful conditions. In the context of climate change, stress resistance is a major concern. To overcome these difficulties, scientists may help breeders by providing genetic markers associated with stress resistance. However, multistress resistance cannot be obtained from the simple addition of single stress resistance traits. In the field, stresses are unpredictable and several may occur at once. Consequently, the use of single stress resistance traits is often inadequate. Although it has been historically linked with the heat stress response, the heat‐shock protein (HSP)/chaperone network is a major component of multiple stress responses. Among the HSP/chaperone ‘client proteins’, many are primary metabolism enzymes and signal transduction components with essential roles for the proper functioning of a cell. HSPs/chaperones are controlled by the action of diverse heat‐shock factors, which are recruited under stress conditions. In this review, we give an overview of the regulation of the HSP/chaperone network with a focus on Arabidopsis thaliana. We illustrate the role of HSPs/chaperones in regulating diverse signalling pathways and discuss several basic principles that should be considered for engineering multiple stress resistance in crops through the HSP/chaperone network.
            Article 0 comments Cited 233 times – based on 0 reviews     Review now
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              The continuing conundrum of the LEA proteins.

              Alan Tunnacliffe, Michael Wise (2007)
              Research into late embryogenesis abundant (LEA) proteins has been ongoing for more than 20 years but, although there is a strong association of LEA proteins with abiotic stress tolerance particularly dehydration and cold stress, for most of that time, their function has been entirely obscure. After their initial discovery in plant seeds, three major groups (numbered 1, 2 and 3) of LEA proteins have been described in a range of different plants and plant tissues. Homologues of groups 1 and 3 proteins have also been found in bacteria and in certain invertebrates. In this review, we present some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlight several possible functions. These include roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as "space fillers" to prevent cellular collapse at low water activities. This multifunctional capacity of the LEA proteins is probably attributable in part to their structural plasticity, as they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. The challenge now facing researchers investigating these enigmatic proteins is to make sense of the various in vitro defined functions in the living cell: Are the LEA proteins truly multi-talented, or are they still just misunderstood?
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                Author and article information

                Journal
                Journal ID (nlm-ta): Proteomes
                Journal ID (iso-abbrev): Proteomes
                Journal ID (publisher-id): proteomes
                Title: Proteomes
                Publisher: MDPI
                ISSN (Electronic): 2227-7382
                Publication date (Electronic): 28 July 2017
                Publication date Collection: September 2017
                Volume: 5
                Issue: 3
                Electronic Location Identifier: 19
                Affiliations
                [1 ]Institut des Sciences Exactes et Appliquées (EA 7484), Université de Nouvelle-Calédonie, BP R4, 98851 Nouméa, Nouvelle-Calédonie; mvillegente@ 123456gmail.com (M.V.); valerie.sarramegna@ 123456univ-nc.nc (V.S.-B.)
                [2 ]Institut de recherche pour le développement (IRD), UMR Diversité, Adaptation et Développement des plantes (DIADE), BP A5, 98848 Nouméa Cedex, Nouvelle-Calédonie
                [3 ]Centre National de la Recherche Scientifique (CNRS), CNRS-Université Claude Bernard Lyon-Institut National des Sciences Appliquées-Bayer CropScience (UMR5240), Bayer CropScience, F-69263 Lyon CEDEX 9, France; claudette.job@ 123456gmail.com
                [4 ]IJPB, Institut Jean-Pierre Bourgin (Institut National de la Rechercherche Agronomique(INRA), AgroParisTech, CNRS, Université Paris-Saclay) ; « Saclay Plant Sciences (SPS) » - RD10, F-78026 Versailles, France; mgalland1983@ 123456gmail.com (M.G.); gwendal.cueff@ 123456agroparistech.fr (G.C.); beatrice.godin@ 123456versailles.inra.fr (B.G.); loic.rajjou@ 123456agroparistech.fr (L.R.)
                [5 ]AgroParisTech, Département « Science de la Vie et Santé », Unité de Formation-Recherche en Physiologie végétale, F-75231 Paris, France
                [6 ]Plateforme d'Analyse Protéomique de Paris Sud Ouest (PAPPSO), GQE–Le Moulon, INRA, Université Paris-Sud, CNRS, AgroParisTech, Université Paris-Saclay, F-91190 Gif-sur-Yvette, France; balliau@ 123456moulon.inra.fr (T.B.); zivy@ 123456moulon.inra.fr (M.Z.)
                [7 ]Institut Agronomique Néo-Calédonien (IAC), Équipe ARBOREAL, Agriculture Biodiversité et Valorisation, BP 73 Port Laguerre, 98890 Païta, Nouvelle-Calédonie
                Author notes
                Author information
                https://orcid.org/0000-0003-2178-1689
                Article
                Publisher ID: proteomes-05-00019
                DOI: 10.3390/proteomes5030019
                PMC ID: 5620536
                PubMed ID: 28788068
                SO-VID: 6964f8e1-7b17-4c42-8a82-1d88229f1394
                Copyright © © 2017 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 30 June 2017
                Date accepted : 25 July 2017
                Categories
                Subject: Article

                Keywords: amborella trichopoda,basal angiosperms,seeds,desiccation tolerance,proteomics
                Data availability:
                Keywords: amborella trichopoda, basal angiosperms, seeds, desiccation tolerance, proteomics

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