Search

Your search keyword '"Giulio Rocco Stella"' showing total 5 results
Start Over Author "Giulio Rocco Stella"
5 results on '"Giulio Rocco Stella"'

1. Engineering the Unicellular Alga Phaeodactylum tricornutum for Enhancing Carotenoid Production

Author

Francesco Manfellotto, Giulio Rocco Stella, Angela Falciatore, Christophe Brunet, and Maria Immacolata Ferrante

Subjects
diatoms, Phaeodacytlum tricornutum, carotenoids, fucoxanthin, genetic engineering, Therapeutics. Pharmacology, RM1-950
Abstract

Microalgae represent a promising resource for the production of beneficial natural compounds due to their richness in secondary metabolites and easy cultivation. Carotenoids feature among distinctive compounds of many microalgae, including diatoms, which owe their golden color to the xanthophyll fucoxanthin. Carotenoids have antioxidant, anti-obesity and anti-inflammatory properties, and there is a considerable market demand for these compounds. Here, with the aim to increase the carotenoid content in the model diatom Phaeodactylum tricornutum, we exploited genetic transformation to overexpress genes involved in the carotenoid biosynthetic pathway. We produced transgenic lines over-expressing simultaneously one, two or three carotenoid biosynthetic genes, and evaluated changes in pigment content with high-performance liquid chromatography. Two triple transformants over-expressing the genes Violaxanthin de-epoxidase (Vde), Vde-related (Vdr) and Zeaxanthin epoxidase 3 (Zep3) showed an accumulation of carotenoids, with an increase in the fucoxanthin content up to four fold. Vde, Vdr and Zep3 mRNA and protein levels in the triple transformants were coherently increased. The exact role of these enzymes in the diatom carotenoid biosynthetic pathway is not completely elucidated nevertheless our strategy successfully modulated the carotenoid metabolism leading to an accumulation of valuable compounds, leading the way toward improved utilization of microalgae in the field of antioxidants.

Published
2020
Full Text
View/download PDF

2. Dynamic changes between two LHCX-related energy quenching sites control diatom photoacclimation

Author

Marianne Jaubert, Herbert van Amerongen, Jean-Pierre Bouly, Giulio Rocco Stella, Bernard Lepetit, Angela Falciatore, Roberto Bassi, Giovanni Finazzi, Volha U. Chukhutsina, Lucilla Taddei, Biologie Computationnelle et Quantitative = Laboratory of Computational and Quantitative Biology (LCQB), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratory of Biophysics and MicroSpectroscopy Research Facility, Wageningen University, LaserLaB Vrije Universiteit Amsterdam (LaserLaB), Vrije Universiteit Amsterdam [Amsterdam] (VU), Department of Physics and Astronomy [Amsterdam], Department of Plant Ecophysiology, University of Konstanz, Department of Biotechnology [Verona] (UNIVR | DBT), University of Verona (UNIVR), Physiologie cellulaire et végétale (LPCV), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Marie Curie Initial Training Network Accliphot (FP7-PEPOPLE-2012- ITN, 316427), Marie Curie Initial Training Network CALIPSO (ITN 2013 GA 607607), Human Frontier Science Program (HFSP0052), Zukunftskolleg Konstanz and the Deutsche Forschungsgemeinschaft (DFG-LE 3358/3-1), ANR-12-BIME-0005,DiaDomOil,Domestication des diatomées pour la production de biocarburants(2012), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Department of Biotechnology, University of Verona, Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-12- BIME-0005,DiaDomOil,DiaDomOil, ANR-10- LABX-49-01,Labex GRAL,Labex GRAL, Biophysics Photosynthesis/Energy, LaserLaB - Energy, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), and Università degli studi di Verona = University of Verona (UNIVR)

Subjects
Chlorophyll, 0106 biological sciences, 0301 basic medicine, Chloroplasts, Light, Photosystem II, Physiology, Acclimatization, Light-Harvesting Protein Complexes, LHCX1, Plant Science, 01 natural sciences, Phaeodactylum tricornutum, Energy quenching, algae, diatoms, photosynthesis, Protein Isoforms, Photosynthesis, algae, chemistry.chemical_classification, biology, Chemistry, Articles, Photochemical Processes, Biofysica, Gene Knockdown Techniques, Light acclimation, Biophysics, Chloroplast, Fluorescence, diatoms, 03 medical and health sciences, Genetics, Life Science, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, SDG 14 - Life Below Water, Marine diatoms, VLAG, Quenching (fluorescence), Organisms, Genetically Modified, fungi, Non photochemical quenching, Photosystem II Protein Complex, biology.organism_classification, 030104 developmental biology, Diatom, Gene Expression Regulation, Xanthophyll, Photoprotection, EPS, 010606 plant biology & botany
Abstract

International audience; Marine diatoms are prominent phytoplankton organisms that perform photosynthesis in extremely variable environments. Diatoms possess a strong ability to dissipate excess absorbed energy as heat via nonphotochemical quenching (NPQ). This process relies on changes in carotenoid pigment composition (xanthophyll cycle) and on specific members of the light-harvesting complex family specialized in photoprotection (LHCXs), which potentially act as NPQ effectors. However, the link between light stress, NPQ, and the existence of different LHCX isoforms is not understood in these organisms. Using picosecond fluorescence analysis, we observed two types of NPQ in the pennate diatom Phaeodactylum tricornutum that were dependent on light conditions. Short exposure of low-light-acclimated cells to high light triggers the onset of energy quenching close to the core of photosystem II, while prolonged light stress activates NPQ in the antenna. Biochemical analysis indicated a link between the changes in the NPQ site/mechanism and the induction of different LHCX isoforms, which accumulate either in the antenna complexes or in the core complex. By comparing the responses of wild-type cells and transgenic lines with a reduced expression of the major LHCX isoform, LHCX1, we conclude that core complex-associated NPQ is more effective in photoprotection than is the antenna complex. Overall, our data clarify the complex molecular scenario of light responses in diatoms and provide a rationale for the existence of a degenerate family of LHCX proteins in these algae.

Published
2018
Full Text
View/download PDF

3. LHCSR Expression under HSP70/RBCS2 Promoter as a Strategy to Increase Productivity in Microalgae

Author

Matteo Ballottari, Federico Perozeni, and Giulio Rocco Stella

Subjects
0106 biological sciences, 0301 basic medicine, light harvesting, microalgae, non-photochemical quenching, photoprotection, photosynthesis, plant biotechnology, Pigment binding, Light-Harvesting Protein Complexes, Chlamydomonas reinhardtii, Biomass, Photosynthetic efficiency, Photosynthesis, 01 natural sciences, Catalysis, Article, Inorganic Chemistry, lcsh:Chemistry, 03 medical and health sciences, HSP70 Heat-Shock Proteins, Physical and Theoretical Chemistry, Promoter Regions, Genetic, Molecular Biology, lcsh:QH301-705.5, Spectroscopy, biology, Chemistry, Non-photochemical quenching, Organic Chemistry, RuBisCO, General Medicine, biology.organism_classification, Computer Science Applications, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, Photoprotection, biology.protein, Biophysics, 010606 plant biology & botany, Biotechnology
Abstract

Microalgae are unicellular photosynthetic organisms considered as potential alternative sources for biomass, biofuels or high value products. However, limited biomass productivity is commonly experienced in their cultivating system despite their high potential. One of the reasons for this limitation is the high thermal dissipation of the light absorbed by the outer layers of the cultures exposed to high light caused by the activation of a photoprotective mechanism called non-photochemical quenching (NPQ). In the model organism for green algae Chlamydomonas reinhardtii, NPQ is triggered by pigment binding proteins called light-harvesting-complexes-stress-related (LHCSRs), which are over-accumulated in high light. It was recently reported that biomass productivity can be increased both in microalgae and higher plants by properly tuning NPQ induction. In this work increased light use efficiency is reported by introducing in C. reinhardtii a LHCSR3 gene under the control of Heat Shock Protein 70/RUBISCO small chain 2 promoter in a npq4 lhcsr1 background, a mutant strain knockout for all LHCSR genes. This complementation strategy leads to a low expression of LHCSR3, causing a strong reduction of NPQ induction but is still capable of protecting from photodamage at high irradiance, resulting in an improved photosynthetic efficiency and higher biomass accumulation.

Published
2018
Full Text
View/download PDF

4. A systems-wide understanding of photosynthetic acclimation in algae and higher plants

Author

Roberto Bassi, Ioannis Dikaios, Brieuc Urbain, Michel Goldschmidt-Clermont, Oliver Ebenhöh, Anna Matuszyńska, Stephanie Spelberg, Julie Maguire, Kailash Adhikari, Adeline Le Monnier, Dipali Singh, Stefano Magni, Giulio Rocco Stella, Lucilla Taddei, Federica Cariti, Claudia Zabke, Fiona Wanjiku Moejes, Antonella Succurro, Kathrin Müller, Giovanni Finazzi, Mark G. Poolman, Valeria Villanova, Serena Flori, Guillaume Cogne, Angela Falciatore, Cluster of Excellence on Plant Sciences (CEPLAS), Institute of Quantitative and Theoretical Biology, Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Bantry Marine Research Station, Department of Biological and Medical Sciences, Oxford Brookes University, Department of Biotechnology, University of Tehran-University College of Science, Department of Botany and Plant Biology, University of Geneva, Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Institut Universitaire de Technologie - Nantes (IUT Nantes), Université de Nantes (UN)-Université de Nantes (UN)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique Bretagne-Pays de la Loire (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Institut Universitaire de Technologie - La Roche-sur-Yon (IUT La Roche-sur-Yon), Université de Nantes (UN), Centre National de la Recherche Scientifique (CNRS), Ecole Nationale Vétérinaire Agroalimentaire et de l'Alimentation Nantes Atlantique (ONIRIS), PRES Université Nantes Angers Le Mans (UNAM), Biologie Computationnelle et Quantitative = Laboratory of Computational and Quantitative Biology (LCQB), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC), Sorbonne Université (SU), UMR 1417 PCV Laboratoire de Physiologie Cellulaire Végétale., Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut National de la Recherche Agronomique (INRA), Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Fermentalg SA, IMT Atlantique Bretagne-Pays de la Loire (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT), University of Aberdeen, Marie Curie Initial Training Network project, AccliPhot [PITN-GA-2012-316427], Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-IMT Atlantique Bretagne-Pays de la Loire (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Centre National de la Recherche Scientifique (CNRS)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-Université de Nantes (UN)-Institut Universitaire de Technologie - Nantes (IUT Nantes), Université de Nantes (UN)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Institut Universitaire de Technologie - La Roche-sur-Yon (IUT La Roche-sur-Yon), Université de Nantes (UN)-Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Université Bretagne Loire (UBL), Heinrich-Heine-Universität Düsseldorf [Düsseldorf], Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie (Paris 6), Sorbonne Universités, Université Grenoble Alpes (UGA), Ecole Nationale Supérieure des Mines de Nantes (Mines Nantes), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique (IMT Atlantique), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), IMT Atlantique (IMT Atlantique), Moejes F.W., Matuszynska A., Adhikari K., Bassi R., Cariti F., Cogne G., Dikaios I., Falciatore A., Finazzi G., Flori S., Goldschmidt-Clermont M., Magni S., Maguire J., Le Monnier A., Muller K., Poolman M., Singh D., Spelberg S., Stella G.R., Succurro A., Taddei L., Urbain B., Villanova V., Zabke C., and Ebenhoh O.

Subjects
0301 basic medicine, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, Physiology, Acclimatization, Context (language use), PhD training, interdisciplinary training, Plant Science, Biochemistry, biophysics & molecular biology [F05] [Life sciences], Biology, acclimation, Photosynthesis, Models, Biological, modelling, 03 medical and health sciences, Algae, Chlorophyta, application industrielle, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, mathematical modelling, Biochimie, biophysique & biologie moléculaire [F05] [Sciences du vivant], biodiversity, modélisation, micro-algue, Phototroph, photosynthetic system, Ecology, Non-photochemical quenching, Systems Biology, acclimatation photosynthétique, photosynthetic optimisation, Plankton, Plants, analyse rétrospective, biology.organism_classification, industrial application, European Training Network, 030104 developmental biology, Acclimation, microalgal cultivation, non-photochemical quenching, Photosynthetic acclimation, adaptation à la lumière, appareil photosynthétique, Biochemical engineering
Abstract

The ability of phototrophs to colonise different environments relies on robust protection against oxidative stress, a critical requirement for the successful evolutionary transition from water to land. Photosynthetic organisms have developed numerous strategies to adapt their photosynthetic apparatus to changing light conditions in order to optimise their photosynthetic yield, which is crucial for life on Earth to exist. Photosynthetic acclimation is an excellent example of the complexity of biological systems, where highly diverse processes, ranging from electron excitation over protein protonation to enzymatic processes coupling ion gradients with biosynthetic activity, interact on drastically different timescales from picoseconds to hours. Efficient functioning of the photosynthetic apparatus and its protection is paramount for efficient downstream processes, including metabolism and growth. Modern experimental techniques can be successfully integrated with theoretical and mathematical models to promote our understanding of underlying mechanisms and principles. This review aims to provide a retrospective analysis of multidisciplinary photosynthetic acclimation research carried out by members of the Marie Curie Initial Training Project, AccliPhot, placing the results in a wider context. The review also highlights the applicability of photosynthetic organisms for industry, particularly with regards to the cultivation of microalgae. It intends to demonstrate how theoretical concepts can successfully complement experimental studies broadening our knowledge of common principles in acclimation processes in photosynthetic organisms, as well as in the field of applied microalgal biotechnology.

Published
2017
Full Text
View/download PDF

5. Identification of pH-sensing Sites in the Light Harvesting Complex Stress-related 3 Protein Essential for Triggering Non-photochemical Quenching in Chlamydomonas reinhardtii

Author

Thuy B. Truong, Giulio Rocco Stella, Erika Erickson, Graham R. Fleming, Eleonora De Re, Roberto Bassi, Krishna K. Niyogi, Matteo Ballottari, Biologie Computationnelle et Quantitative = Laboratory of Computational and Quantitative Biology (LCQB), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), U.S. Department of Energy, Office of Science, Basic Energy Sciences, Chemical Sciences, Geosciences, and Biosciences Division [449B], Italian Ministry of Education, University and Research through PRIN ('Progetti di Ricerca di Interesse Nazionale') [2012XSAWYM], National Science Foundation, Marie Curie Actions Initial Training Networks ACCLIPHOT [PITN-GA-2012-316427], Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, 0301 basic medicine, Biochemistry & Molecular Biology, Photosystem II, [SDV]Life Sciences [q-bio], Mutant, Light-Harvesting Protein Complexes, Mutation, Missense, Chlamydomonas reinhardtii, Plant Biology, Biology, 01 natural sciences, Biochemistry, Medical and Health Sciences, Thylakoids, Light-harvesting complex, 03 medical and health sciences, Affordable and Clean Energy, Site-Directed, Asparagine, Molecular Biology, fluorescence, non-photochemical quenching, photoprotection, photosynthesis, photosynthetic pigment, photosystem II, plant biochemistry, Hydrogen-Ion Concentration, Mutagenesis, Site-Directed, Non-photochemical quenching, Cell Biology, Biological Sciences, biology.organism_classification, 030104 developmental biology, Mutagenesis, Photoprotection, Thylakoid, Chemical Sciences, Mutation, Missense, 010606 plant biology & botany
Abstract

International audience; Light harvesting complex stress-related 3 (LHCSR3) is the protein essential for photoprotective excess energy dissipation (non-photochemical quenching, NPQ) in the model green alga Chlamydomonas reinhardtii. Activation of NPQ requires low pH in the thylakoid lumen, which is induced in excess light conditions and sensed by lumen-exposed acidic residues. In this work we have used site-specific mutagenesis in vivo and in vitro for identification of the residues in LHCSR3 that are responsible for sensing lumen pH. Lumen-exposed protonatable residues, aspartate and glutamate, were mutated to asparagine and glutamine, respectively. By expression in a mutant lacking all LHCSR isoforms, residues Asp(117), Glu(221), and Glu(224) were shown to be essential for LHCSR3-dependent NPQ induction in C. reinhardtii. Analysis of recombinant proteins carrying the same mutations refolded in vitro with pigments showed that the capacity of responding to low pH by decreasing the fluorescence life time, present in the wild-type protein, was lost. Consistent with a role in pH sensing, the mutations led to a substantial reduction in binding the NPQ inhibitor dicyclohexylcarbodiimide.

Published
2016
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results