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The realisation of the full objectives of international policies targeting global food security and climate change mitigation, including the European Green Deal, United Nation’s Sustainable Development Goals (SDGs), the Paris Climate Agreement COP21 and transition away from a fossil-carbon industrial base to one that is more bio-based, requires that we (i) sustainably increase the yield, nutritional quality, and biodiversity of major crop species, (ii) select climate-ready crops that are adapted to future weather dynamic and (iii) increase the resource use efficiency of crops to preserve natural resources, such as fresh water and phosphate and reducing the environmental burden arising from the application of nitrogenous fertiliser. Advanced scientific knowledge and tools for research and crop breeding already provide an excellent platform to build on. A long-term Strategic Research Agenda now needs to be agreed and priorities set to deliver blueprints for climate resilient future-proofed crops. This strategy should then be implemented through an innovative collaborative approach that combines the joint knowledge base of the research and industrial communities, with multi-stakeholder involvement and strong support from policy makers. This white paper has been compiled from contributions from several experts across the field of plant sciences. The CropBooster-P project has developed this strategic research agenda for a crop improvement programme that will provide the genetic innovation to improve and future proof our crop plants. It builds a strong collaboration between plant scientists and modellers, physicists, soil scientists, engineers and coders, biomathematicians, agronomists, plant breeders and farmers. The goal is to exploit the largely untapped genetic diversity that exists within the wild relatives and ancient and heirloom varieties of our crop plants to improve our crops so they will be more resilient, high yielding, resource efficient, nutritious, and ready for the future climate of Europe. The knowledge and technology to reach this goal springs from the transformative developments that have occurred in the last 20 years in genomics, phenomics, crop sciences, molecular plant sciences, agronomy, and plant breeding.

© 2020 The Authors. Plant Direct published by American Society of Plant Biologists and the Society for Experimental Biology and John Wiley & Sons Ltd The multinational Arabidopsis research community is highly collaborative and over the past thirty years these activities have been documented by the Multinational Arabidopsis Steering Committee (MASC). Here, we (a) highlight recent research advances made with the reference plant Arabidopsis thaliana; (b) provide summaries from recent reports submitted by MASC subcommittees, projects and resources associated with MASC and from MASC country representatives; and (c) initiate a call for ideas and foci for the “fourth decadal roadmap,” which will advise and coordinate the global activities of the Arabidopsis research community.

International audience; Chloroplasts are major components of plant cells. Such plastids fulfill many crucial functions, such as assimilation of carbon, sulfur and nitrogen as well as synthesis of essential metabolites. These organelles consist of the following three key sub-compartments. The envelope, characterized by two membranes, surrounds the organelle and controls the communication of the plastid with other cell compartments. The stroma is the soluble phase of the chloroplast and the main site where carbon dioxide is converted into carbohydrates. The thylakoid membrane is the internal membrane network consisting of grana (flat compressed sacs) and lamellae (less dense structures), where oxygenic photosynthesis takes place. The present protocol describes step by step procedures required for the purification, using differential centrifugations and Percoll gradients, of intact chloroplasts from Arabidopsis, and their fractionation, using sucrose gradients, in three sub-compartments (i.e., envelope, stroma, and thylakoids). This protocol also provides instructions on how to assess the purity of these fractions using markers associated to the various chloroplast sub-compartments. The method described here is valuable for subplastidial localization of proteins using immunoblotting, but also for subcellular and subplastidial proteomics and other studies.

International audience; Enzymatic and non-enzymatic peroxidation of polyunsaturated fatty acids give rise to accumulation of aldehydes, ketones, and alpha, beta-unsaturated carbonyls of various lengths, known as oxylipins. Oxylipins with alpha, beta-unsaturated carbonyls are reactive electrophile species and are toxic. Cells have evolved several mechanisms to scavenge reactive electrophile oxylipins and decrease their reactivity such as by coupling with glutathione, or by reduction using NAD(P)H-dependent reductases and dehydrogenases of various substrate specificities. Plant cell chloroplasts produce reactive electrophile oxylipins named gamma-ketols downstream of enzymatic lipid peroxidation. The chloroplast envelope quinone oxidoreductase homolog (ceQORH) from Arabidopsis thaliana was previously shown to reduce the reactive double bond of gamma-ketols. In marked difference with its cytosolic homolog alkenal reductase (AtAER) that displays a high activity toward the ketodiene 13-oxo-9(Z), 11(E)-octadecadienoic acid (13-KODE) and the ketotriene 13-oxo-9(Z), 11(E), 15(Z)-octadecatrienoic acid (13-KOTE), ceQORH binds, but does not reduce, 13-KODE and 13-KOTE. Crystal structures of apo-ceQORH and ceQORH bound to 13-KOTE or to NADP(+) and 13-KOTE have been solved showing a large ligand binding site, also observed in the structure of the cytosolic alkenal/one reductase. Positioning of the alpha, beta-unsaturated carbonyl of 13-KOTE in ceQORH-NADP(+)-13-KOTE, far away from the NADP(+) nicotinamide ring, provides a rational for the absence of activity with the ketodienes and ketotrienes. ceQORH is a monomeric enzyme in solution whereas other enzymes from the quinone oxidoreductase family are stable dimers and a structural explanation of this difference is proposed. A possible in vivo role of ketodienes and ketotrienes binding to ceQORH is also discussed.