Search results for "Protein Complex"

showing 10 items of 154 documents

GreenCut proteinCPLD49 ofChlamydomonas reinhardtiiassociates with thylakoid membranes and is required for cytochromeb6fcomplex accumulation

2018

The GreenCut encompasses a suite of nucleus-encoded proteins with orthologs among green lineage organisms (plants, green algae), but that are absent or poorly conserved in non-photosynthetic/heterotrophic organisms. In Chlamydomonas reinhardtii, CPLD49 (Conserved in Plant Lineage and Diatoms49) is an uncharacterized GreenCut protein that is critical for maintaining normal photosynthetic function. We demonstrate that a cpld49 mutant has impaired photoautotrophic growth under high-light conditions. The mutant exhibits a nearly 90% reduction in the level of the cytochrome b6 f complex (Cytb6 f), which impacts linear and cyclic electron transport, but does not compromise the ability of the stra…

0106 biological sciences0301 basic medicineCytochrome b6f complex[SDV]Life Sciences [q-bio]MutantChlamydomonas reinhardtii[SDV.BC]Life Sciences [q-bio]/Cellular BiologyCell BiologyPlant ScienceBiologyPhotosynthesisbiology.organism_classification01 natural sciencesElectron transport chainCell biologyChloroplast03 medical and health sciences030104 developmental biologyMembrane protein complexThylakoidGeneticsComputingMilieux_MISCELLANEOUS010606 plant biology & botanyThe Plant Journal
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The Nonbilayer Lipid MGDG and the Major Light-Harvesting Complex (LHCII) Promote Membrane Stacking in Supported Lipid Bilayers.

2018

The thylakoid membrane of algae and land plants is characterized by its intricate architecture, comprising tightly appressed membrane stacks termed grana. The contributions of individual components to grana stack formation are not yet fully elucidated. As an in vitro model, we use supported lipid bilayers made of thylakoid lipid mixtures to study the effect of major light-harvesting complex (LHCII), different lipids, and ions on membrane stacking, seen as elevated structures forming on top of the planar membrane surface in the presence of LHCII protein. These structures were examined by confocal laser scanning microscopy, atomic force microscopy, and fluorescence recovery after photobleachi…

0106 biological sciences0301 basic medicineMicroscopy ConfocalChemistryLipid BilayersStackingLight-Harvesting Protein ComplexesPeasfood and beveragesFluorescence recovery after photobleachingMicroscopy Atomic Force01 natural sciencesBiochemistryLight-harvesting complexDiglycerides03 medical and health sciences030104 developmental biologyGlycolipidMembraneThylakoidConfocal laser scanning microscopyBiophysicslipids (amino acids peptides and proteins)Lipid bilayer010606 plant biology & botanyBiochemistry
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Sorting Motifs Involved in the Trafficking and Localization of the PIN1 Auxin Efflux Carrier

2016

In contrast with the wealth of recent reports about the function of μ-adaptins and clathrin adaptor protein (AP) complexes, there is very little information about the motifs that determine the sorting of membrane proteins within clathrin-coated vesicles in plants. Here, we investigated putative sorting signals in the large cytosolic loop of the Arabidopsis (Arabidopsis thaliana) PIN-FORMED1 (PIN1) auxin transporter, which are involved in binding μ-adaptins and thus in PIN1 trafficking and localization. We found that Phe-165 and Tyr-280, Tyr-328, and Tyr-394 are involved in the binding of different μ-adaptins in vitro. However, only Phe-165, which binds μA(μ2)- and μD(μ3)-adaptin, was found …

0106 biological sciences0301 basic medicinePhysiologyPhenylalanineGreen Fluorescent ProteinsMutantArabidopsisPlant ScienceProtein Sorting SignalsEndoplasmic ReticulumEndocytosis01 natural sciencesClathrin03 medical and health sciencesCytosolGeneticsGuanine Nucleotide Exchange FactorsSecretory pathwaybiologyArabidopsis ProteinsEndoplasmic reticulumMembrane Transport ProteinsSignal transducing adaptor proteinArticlesPlants Genetically ModifiedClathrinEndocytosisAdaptor Protein Complex mu SubunitsTransport proteinCell biologyProtein Transport030104 developmental biologyProtein Sorting SignalsMutationbiology.protein010606 plant biology & botanyPlant Physiology
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UV-screening and springtime recovery of photosynthetic capacity in leaves of Vaccinium vitis-idaea above and below the snow pack

2019

International audience; Evergreen plants in boreal biomes undergo seasonal hardening and dehardening adjusting their photosynthetic capacity and photoprotection; acclimating to seasonal changes in temperature and irradiance. Leaf epidermal ultraviolet (UV)-screening by flavonols responds to solar radiation, perceived in part through increased ultraviolet-B (UV-B) radiation, and is a candidate trait to provide cross-photoprotection. At Hyytiälä Forestry Station, central Finland, we examined whether the accumulation of flavonols was higher in leaves of Vaccinium vitis-idaea L. growing above the snowpack compared with those below the snowpack. We found that leaves exposed to colder temperature…

0106 biological sciences0301 basic medicineTime FactorsPhotoinhibitionBOREALPhysiologyPlant ScienceForests01 natural sciencesPlant EpidermisAnthocyaninsSoilFlavonolsLOW-TEMPERATURESnowPhotosynthesis1183 Plant biology microbiology virologychemistry.chemical_classificationspring dehardening.CLIMATE-CHANGEbiologyChemistryTemperatureUnderstoreyHorticultureLIGHTSeasonsVacciniumUltraviolet RaysGrowing seasonPhotosynthesisDWARF SHRUB03 medical and health sciencesLEAFPHOTOSYSTEM-IIGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyVaccinium vitis-idaeaFlavonoidsSpring dehardeningPhotoprotectionSpectral qualityPhotosystem II Protein ComplexPigments Biological15. Life on landEvergreenbiology.organism_classificationPhotosynthetic capacitySUB-ARCTIC HEATHPlant Leaves030104 developmental biology13. Climate actionPhotoprotectionWINTERB RADIATIONArctic browning010606 plant biology & botany
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Plant Responses to Abiotic Stress Regulated by Histone Deacetylases

2017

In eukaryotic cells, histone acetylation and deacetylation play an important role in the regulation of gene expression. Histone acetylation levels are modulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs). Recent studies indicate that HDACs play essential roles in the regulation of gene expression in plant response to environmental stress. In this review, we discussed the recent advance regarding the plant HDACs and their functions in the regulation of abiotic stress responses. The role of HDACs in autophagy was also discussed.

0106 biological sciences0301 basic medicineautophagyabiotic stressHistone acetylation and deacetylationMini ReviewPlant Sciencelcsh:Plant culture01 natural sciencesEnvironmental stress03 medical and health scienceschemistry.chemical_compoundhistone deacetylationlcsh:SB1-1110Histone AcetyltransferasesRegulation of gene expressionprotein complexesbiologyAbiotic stressAutophagyHDACsCell biology030104 developmental biologyHistonechemistryAcetylationbiology.protein010606 plant biology & botanyFrontiers in Plant Science
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Arabidopsis RCD1 coordinates chloroplast and mitochondrial functions through interaction with ANAC transcription factors

2019

Reactive oxygen species (ROS)-dependent signaling pathways from chloroplasts and mitochondria merge at the nuclear protein RADICAL-INDUCED CELL DEATH1 (RCD1). RCD1 interacts in vivo and suppresses the activity of the transcription factors ANAC013 and ANAC017, which mediate a ROS-related retrograde signal originating from mitochondrial complex III. Inactivation of RCD1 leads to increased expression of mitochondrial dysfunction stimulon (MDS) genes regulated by ANAC013 and ANAC017. Accumulating MDS gene products, including alternative oxidases (AOXs), affect redox status of the chloroplasts, leading to changes in chloroplast ROS processing and increased protection of photosynthetic apparatus.…

0106 biological sciences0301 basic medicineretrograde signalingChloroplastsArabidopsisPlant BiologyMitochondrion01 natural sciencesElectron Transport Complex IIIGene Expression Regulation PlantArabidopsisOXIDATIVE STRESS-RESPONSETranscriptional regulationCYCLIC ELECTRON FLOWBiology (General)Nuclear proteinANAC transcription factors1183 Plant biology microbiology virologyreactive oxygen speciesbiologyChemistryRETROGRADE REGULATIONGeneral NeuroscienceQRNuclear Proteinsfood and beveragesGeneral MedicinePlants Genetically Modified:Science::Biological sciences [DRNTU]Cell biologyMitochondriaChloroplastviherhiukkasetMedicineSignal transductionmitochondrial functionsResearch ArticleSignal TransductionQH301-705.5SciencemitokondriotGenetics and Molecular BiologyGeneral Biochemistry Genetics and Molecular BiologyPROTEIN COMPLEXESSIGNALING PATHWAYS03 medical and health scienceschloroplastStress PhysiologicalALTERNATIVE OXIDASESkasvitENZYME-ACTIVITIESredox signalingTranscription factorarabidopsis RCD1General Immunology and MicrobiologybiokemiaArabidopsis Proteinsta1182Biology and Life Sciencesbiology.organism_classification030104 developmental biologyCELL-DEATHPLANT-MITOCHONDRIAA. thalianaGeneral BiochemistryRetrograde signalingGENES-ENCODING MITOCHONDRIALproteiinit010606 plant biology & botanyTranscription Factors
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Chlorophyll fluorescence emission spectrum inside a leaf

2008

International audience; Chlorophyll a fluorescence can be used as an early stress indicator. Fluorescence is also connected to photosynthesis so it can be proposed for global monitoring of vegetation status from a satellite platform. Nevertheless, the correct interpretation of fluorescence requires accurate physical models. The spectral shape of the leaf fluorescence free of any re-absorption effect plays a key role in the models and is difficult to measure. We present a vegetation fluorescence emission spectrum free of re-absorption based on a combination of measurements and modelling. The suggested spectrum takes into account the photosystem I and II spectra and their relative contributio…

0106 biological sciencesChlorophyllChlorophyll aSpectral shape analysisI REACTION CENTERSSPINACH THYLAKOID MEMBRANES[SDU.ASTR.EP]Sciences of the Universe [physics]/Astrophysics [astro-ph]/Earth and Planetary Astrophysics [astro-ph.EP]PHOTOSYNTHETIC MEMBRANEPhotosystem I01 natural sciencesSpectral lineHIGHER-PLANTSPROTEIN COMPLEXES03 medical and health scienceschemistry.chemical_compoundmedicineEmission spectrumPhysical and Theoretical ChemistryChlorophyll fluorescenceLIGHT-HARVESTING COMPLEX030304 developmental biologyRemote sensing0303 health sciencesPhotosystem I Protein Complex[SDU.ASTR]Sciences of the Universe [physics]/Astrophysics [astro-ph]Photosystem II Protein Complexfood and beveragesFluorescencePlant LeavesSpectrometry FluorescenceROOM-TEMPERATUREchemistryPHOTOSYSTEM-I[SDU]Sciences of the Universe [physics]Espectroscòpia de fluorescènciaARABIDOPSIS-THALIANAmedicine.symptomVegetation (pathology)ENERGY-TRANSFER010606 plant biology & botany
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Functional rearrangement of the light-harvesting antenna upon state transitions in a green alga

2014

AbstractState transitions in the green alga Chlamydomonas reinhardtii serve to balance excitation energy transfer to photosystem I (PSI) and to photosystem II (PSII) and possibly play a role as a photoprotective mechanism. Thus, light-harvesting complex II (LHCII) can switch between the photosystems consequently transferring more excitation energy to PSII (state 1) or to PSI (state 2) or can end up in LHCII-only domains. In this study, low-temperature (77 K) steady-state and time-resolved fluorescence measured on intact cells of Chlamydomonas reinhardtii shows that independently of the state excitation energy transfer from LHCII to PSI or to PSII occurs on two main timescales of <15 ps and …

0106 biological sciencesPhotosystem IIEnergy transferBiophysicsLight-Harvesting Protein ComplexesphotosystemChlamydomonas reinhardtiiPhotosystem IPhotochemistry01 natural sciences03 medical and health sciencesstate transitionsgreen algaSDG 7 - Affordable and Clean Energy030304 developmental biologyPhotosystem0303 health sciencesenergy transfer/dk/atira/pure/sustainabledevelopmentgoals/affordable_and_clean_energybiologyPhotosystem I Protein ComplexChemistryta1182Photosystem II Protein ComplexState (functional analysis)biology.organism_classificationFluorescenceCell BiophysicsAtomic physicsExcitationChlamydomonas reinhardtii010606 plant biology & botanyBiophysical journal
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Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis

2020

14 p.-7 fig.-2 tab.

0106 biological sciencesSpliceosomeAcademicSubjects/SCI00010RNA SplicingMutantArabidopsis01 natural sciencesChaperonin//purl.org/becyt/ford/1 [https]03 medical and health sciencesGene Expression Regulation PlantArabidopsisRNA and RNA-protein complexesGeneticsHSP90 Heat-Shock Proteins//purl.org/becyt/ford/1.6 [https]030304 developmental biologyprefoldins0303 health sciencesbiologyArabidopsis ProteinsRNA-Binding Proteinsbiology.organism_classificationHsp903. Good healthCell biologyProteostasisMultiprotein ComplexesMutationRNA splicingSpliceosomesbiology.proteinLSM2-8 complexspliceosomeSmall nuclear RNAMolecular ChaperonesProtein Binding010606 plant biology & botany
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Sorting signals for PIN1 trafficking and localization

2016

PIN-FORMED (PIN) family proteins direct polar auxin transport based on their asymmetric (polar) localization at the plasma membrane. In the case of PIN1, it mainly localizes to the basal (rootward) plasma membrane domain of stele cells in root meristems. Vesicular trafficking events, such as clathrin-dependent PIN1 endocytosis and polar recycling, are probably the main determinants for PIN1 polar localization. However, very little is known about the signals which may be involved in binding the μ-adaptin subunit of clathrin adaptor complexes (APs) for sorting of PIN1 within clathrin-coated vesicles, which can determine its trafficking and localization. We have performed a systematic mutagene…

0301 basic medicineArabidopsis ProteinsVesicleClathrin adaptor complexCell MembraneMembrane Transport ProteinsPlant ScienceBiologyEndocytosisClathrinEndocytosisAdaptor Protein Complex mu SubunitsArticle AddendumCell biologyAdaptor Proteins Vesicular Transport03 medical and health sciences030104 developmental biologybiology.proteinClathrin adaptor proteinsPolar auxin transportTyrosineSecretory pathwayPlant Signaling &amp; Behavior
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