Search results for "Synechocystis"

showing 10 items of 15 documents

The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.

2017

IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contra…

0106 biological sciences0301 basic medicineVesicle-associated membrane protein 8ChloroplastsLipid BilayersBiophysicsBiology01 natural sciencesBiochemistryMembrane FusionThylakoidsArticle03 medical and health sciencesBacterial ProteinsProtein DomainsIntegral membrane proteinMembranesMembrane transport proteinPeripheral membrane proteinSynechocystisLipid bilayer fusionMembrane ProteinsCell BiologyCell biology030104 developmental biologyMembrane proteinMembrane biogenesisbiology.protein010606 plant biology & botanyMembrane Fusion ActivityProtein BindingBiochimica et biophysica acta. Bioenergetics
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Reconstruction and analysis of genome-scale metabolic model of a photosynthetic bacterium

2010

Abstract Background Synechocystis sp. PCC6803 is a cyanobacterium considered as a candidate photo-biological production platform - an attractive cell factory capable of using CO2 and light as carbon and energy source, respectively. In order to enable efficient use of metabolic potential of Synechocystis sp. PCC6803, it is of importance to develop tools for uncovering stoichiometric and regulatory principles in the Synechocystis metabolic network. Results We report the most comprehensive metabolic model of Synechocystis sp. PCC6803 available, iSyn669, which includes 882 reactions, associated with 669 genes, and 790 metabolites. The model includes a detailed biomass equation which encompasses…

0106 biological sciencesSystems biologyIn silicoMetabolic networkComputational biologyBiologyModels Biological01 natural sciencesMetabolic engineeringGene Knockout Techniques03 medical and health sciencesStructural BiologyModelling and Simulation010608 biotechnologyBotanyBiomassPhotosynthesislcsh:QH301-705.5Molecular Biology030304 developmental biologyAutotrophic Processes0303 health sciencesGene Expression ProfilingApplied MathematicsSynechocystisSynechocystisGenomicsDarknessbiology.organism_classificationComputer Science ApplicationsFlux balance analysislcsh:Biology (General)Genes BacterialAutotrophic ProcessesModeling and SimulationEnergy sourceGenome BacterialResearch ArticleBMC Systems Biology
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Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion.

2016

The photosynthetic light reaction takes place within the thylakoid membrane system in cyanobacteria and chloroplasts. Besides its global importance, the biogenesis, maintenance and dynamics of this membrane system are still a mystery. In the last two decades, strong evidence supported the idea that these processes involve IM30, the inner membrane-associated protein of 30kDa, a protein also known as the vesicle-inducing protein in plastids 1 (Vipp1). Even though we just only begin to understand the precise physiological function of this protein, it is clear that interaction of IM30 with membranes is crucial for biogenesis of thylakoid membranes. Here we summarize and discuss forces guiding I…

0301 basic medicineCations DivalentBiophysicsArabidopsisBiologyBiochemistryMembrane FusionThylakoids03 medical and health sciencesBacterial ProteinsPlant CellsMagnesiumPhotosynthesisCytoskeletonPhospholipidsOrganelle BiogenesisMembrane transport proteinArabidopsis ProteinsMembrane structureSynechocystisLipid bilayer fusionMembrane ProteinsCell BiologyCell biology030104 developmental biologyMembraneMembrane proteinThylakoidbiology.proteinOrganelle biogenesisProtein MultimerizationBiogenesisBiochimica et biophysica acta. Biomembranes
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Mg2+ homeostasis and transport in cyanobacteria – at the crossroads of bacterial and chloroplast Mg2+ import

2018

Abstract Magnesium cation (Mg2+) is the most abundant divalent cation in living cells, where it is required for various intracellular functions. In chloroplasts and cyanobacteria, established photosynthetic model systems, Mg2+ is the central ion in chlorophylls, and Mg2+ flux across the thylakoid membrane is required for counterbalancing the light-induced generation of a ΔpH across the thylakoid membrane. Yet, not much is known about Mg2+ homoeostasis, transport and distribution within cyanobacteria. However, Mg2+ transport across membranes has been studied in non-photosynthetic bacteria, and first observations and findings are reported for chloroplasts. Cyanobacterial cytoplasmic membranes…

0301 basic medicineChloroplastsClinical BiochemistryCyanobacteriaPhotosynthesisBiochemistry03 medical and health sciencesHomeostasisMagnesiumElectrochemical gradientMolecular BiologyIon TransportBacteria030102 biochemistry & molecular biologybiologyChemistrySynechocystisMembrane Transport ProteinsMembrane transportbiology.organism_classificationTransmembrane proteinChloroplast030104 developmental biologyMembraneThylakoidBiophysicsBiological Chemistry
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Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and …

2016

The IM30 (inner membrane-associated protein of 30 kDa), also known as the Vipp1 (vesicle-inducing protein in plastids 1), has a crucial role in thylakoid membrane biogenesis and maintenance. Recent results suggest that the protein binds peripherally to membranes containing negatively charged lipids. However, although IM30 monomers interact and assemble into large oligomeric ring complexes with different numbers of monomers, it is still an open question whether ring formation is crucial for membrane interaction. Here we show that binding of IM30 rings to negatively charged phosphatidylglycerol membrane surfaces results in a higher ordered membrane state, both in the head group and in the inn…

0301 basic medicineChloroplastsMembrane lipids02 engineering and technologyBiologyBiochemistryThylakoids03 medical and health scienceschemistry.chemical_compoundMembrane LipidsBacterial ProteinsMembrane BiologyLipid bilayerProtein Structure QuaternaryMolecular BiologyPhosphatidylglycerolSynechocystisMembrane ProteinsBiological membranePhosphatidylglycerolsCell BiologySurface Plasmon Resonance021001 nanoscience & nanotechnologyKinetics030104 developmental biologyMembranechemistryBiochemistryMembrane proteinThylakoidMembrane biogenesisBiophysicsMutant ProteinsProtein Multimerization0210 nano-technologyProtein BindingThe Journal of biological chemistry
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Proton Leakage Is Sensed by IM30 and Activates IM30-Triggered Membrane Fusion

2020

The inner membrane-associated protein of 30 kDa (IM30) is crucial for the development and maintenance of the thylakoid membrane system in chloroplasts and cyanobacteria. While its exact physiological function still is under debate, it has recently been suggested that IM30 has (at least) a dual function, and the protein is involved in stabilization of the thylakoid membrane as well as in Mg2+-dependent membrane fusion. IM30 binds to negatively charged membrane lipids, preferentially at stressed membrane regions where protons potentially leak out from the thylakoid lumen into the chloroplast stroma or the cyanobacterial cytoplasm, respectively. Here we show in vitro that IM30 membrane binding…

0301 basic medicineChloroplastsMembrane lipidsmembrane fusionMg2+CyanobacteriaThylakoidsCatalysisArticleVipp1Inorganic Chemistrylcsh:Chemistry03 medical and health sciencesMembrane Lipidsquartz crystal microbalanceProtein structureBacterial ProteinsPhysical and Theoretical ChemistryMg<sup>2+</sup>membrane bindingMolecular Biologylcsh:QH301-705.5SpectroscopyMembranes030102 biochemistry & molecular biologyChemistrypHOrganic ChemistrySynechocystisCD spectroscopyLipid bilayer fusionMembrane Proteinsfood and beveragesGeneral Medicinethylakoid membraneComputer Science ApplicationsChloroplastChloroplast stroma030104 developmental biologyMembranelcsh:Biology (General)lcsh:QD1-999CytoplasmThylakoidBiophysicsProtonsIM30Protein BindingInternational Journal of Molecular Sciences
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2020

Hsp70 proteins and their Hsp40 co-chaperones are essential components of cellular chaperone networks in both prokaryotes and eukaryotes. Here, we performed a genetic analysis to define the protein domains required for the key functions of the major Hsp40/DnaJ protein Sll0897 of the cyanobacterium Synechocystis sp. PCC6803. The expression of the N-terminally located J- and G/F-domains is essential and sufficient for the proteins' fundamental in vivo functions, whereas the presence of the full-length protein, containing the C-terminal substrate-binding domains, is crucial under stress conditions.

0301 basic medicineCyanobacteriabiologyChemistryProtein domainSynechocystisbiology.organism_classificationDNAJ ProteinGenetic analysisGeneral Biochemistry Genetics and Molecular BiologyHsp70Cell biology03 medical and health sciences030104 developmental biology0302 clinical medicine030220 oncology & carcinogenesisChaperone (protein)biology.proteinViability assayFEBS Open Bio
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Expanding the toolbox for Synechocystis sp. PCC 6803 : validation of replicative vectors and characterization of a novel set of promoters

2018

Cyanobacteria are promising ‘low-cost’ cell factories since they have minimal nutritional requirements, high metabolic plasticity and can use sunlight and CO2 as energy and carbon sources. The unicellular Synechocystis sp. PCC 6803, already considered the ‘green’ Escherichia coli, is the best studied cyanobacterium but to be used as an efficient and robust photoautotrophic chassis it requires a customized and well-characterized toolbox. In this context, we evaluated the possibility of using three self-replicative vectors from the Standard European Vector Architecture (SEVA) repository to transform Synechocystis. Our results demonstrated that the presence of the plasmid does not lead to an e…

0301 basic medicineCyanobacteriapSEVA plasmids030106 microbiologyBiomedical EngineeringHeterologouspromotersBioengineeringContext (language use)Computational biologymedicine.disease_causecyanobacteriaBiomaterials03 medical and health sciencesPlasmidmedicineEscherichia coliGeneQH426synthetic toolboxbiologyChemistrySynechocystisSynechocystisPromoterbiology.organism_classificationAgricultural and Biological Sciences (miscellaneous)3. Good health030104 developmental biologyBiotechnologyResearch Article
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IM30 triggers membrane fusion in cyanobacteria and chloroplasts

2015

The thylakoid membrane of chloroplasts and cyanobacteria is a unique internal membrane system harbouring the complexes of the photosynthetic electron transfer chain. Despite their apparent importance, little is known about the biogenesis and maintenance of thylakoid membranes. Although membrane fusion events are essential for the formation of thylakoid membranes, proteins involved in membrane fusion have yet to be identified in photosynthetic cells or organelles. Here we show that IM30, a conserved chloroplast and cyanobacterial protein of approximately 30 kDa binds as an oligomeric ring in a well-defined geometry specifically to membranes containing anionic lipids. Triggered by Mg2+, membr…

ChloroplastsGeneral Physics and AstronomyBiologyMembrane FusionThylakoidsGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsCentrifugation Density GradientIntegral membrane proteinMultidisciplinaryGalactolipidsPeripheral membrane proteinSynechocystisLipid bilayer fusionfood and beveragesPhosphatidylglycerolsGeneral ChemistryTransmembrane proteinCell biologyChloroplastMembraneThylakoidLiposomesQuantasomeGlycolipidsProtein BindingNature Communications
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The Proteome and Lipidome of Synechocystis sp. PCC 6803 Cells Grown under Light-Activated Heterotrophic Conditions*

2015

Cyanobacteria are photoautotrophic prokaryotes with a plant-like photosynthetic machinery. Because of their short generation times, the ease of their genetic manipulation, and the limited size of their genome and proteome, cyanobacteria are popular model organisms for photosynthetic research. Although the principal mechanisms of photosynthesis are well-known, much less is known about the biogenesis of the thylakoid membrane, hosting the components of the photosynthetic, and respiratory electron transport chain in cyanobacteria. Here we present a detailed proteome analysis of the important model and host organism Synechocystis sp. PCC 6803 under light-activated heterotrophic growth condition…

CyanobacteriaProtein FoldingProteomePhotosynthesisThylakoidsBiochemistryMass SpectrometryAnalytical ChemistryRespiratory electron transport chainMembrane LipidsBacterial ProteinsMolecular BiologybiologyResearchSynechocystisLipidomebiology.organism_classificationCarbonOxidative StressPhototrophic ProcessesMembraneBiochemistryThylakoidProteomeBiogenesisChromatography LiquidMolecular &amp; Cellular Proteomics
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