Search results for "cytochrome b"

showing 10 items of 63 documents

SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH.

2011

Abstract The folding and stabilization of α-helical transmembrane proteins are still not well understood. Following cofactor binding to a membrane protein provides a convenient method to monitor the formation of appropriate native structures. We have analyzed the assembly and stability of the transmembrane cytochrome b 559 ′, which can be efficiently assembled in vitro from a heme-binding PsbF homo-dimer by combining free heme with the apo-cytochrome b 559 ′. Unfolding of the protein dissolved in the mild detergent dodecyl maltoside may be induced by addition of SDS, which at high concentrations leads to dimer dissociation. Surprisingly, absorption spectroscopy reveals that heme binding and…

Models MolecularCofactor bindingProtein FoldingHeme bindingCytochromebiologyChemistryCytochrome bSpectrum AnalysisMembrane ProteinsSodium Dodecyl SulfateHemeCytochromes bHydrogen-Ion ConcentrationTransmembrane proteinchemistry.chemical_compoundBiochemistryStructural Biologybiology.proteinHumansProtein foldingMolecular BiologyHemeHistidineProtein BindingJournal of molecular biology
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Heme Binding Constricts the Conformational Dynamics of the Cytochrome b559′ Heme Binding Cavity

2012

Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. The PsbF polypeptide can dimerize in the absence and presence of heme. To monitor structural alterations associated with binding of heme to the apo-cytochrome, we analyzed the apo- and holo-cytochrome structure by electron paramagnetic resonance spectroscopy. Spin labeling of amino acids located close to the heme binding domain of the cytochrome revealed that the structure of the heme binding domain is unconstrained in the absence of heme. Heme binding restricts the conformational dynamics of the heme binding domain, resulting in the structu…

Models MolecularHemeproteinCytochromeHeme bindingMolecular Sequence DataHemePlasma protein bindingBiochemistryProtein Structure SecondaryCofactorchemistry.chemical_compoundApoenzymesAmino Acid SequenceGlycophorinsHemebiologyCytochrome bCell MembraneElectron Spin Resonance SpectroscopyTemperaturePhotosystem II Protein ComplexSite-directed spin labelingCytochrome b GroupProtein Structure Tertiarychemistrybiology.proteinBiophysicsSpin LabelsPeptidesProtein BindingBiochemistry
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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

2012

AbstractWhen localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b559′ to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser…

Models MolecularProlineHeme bindingStereochemistryDimerMolecular ConformationBiophysicsCofactor bindingHemeBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureProtein stabilitySerineProtein foldingCofactor bindingHydrogen bondCell MembranePhotosystem II Protein ComplexHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinProtein Structure TertiaryOxygenTransmembrane domainHelix interactionchemistrySpectrophotometryMembrane proteinMutationTransmembrane helixProtein foldingDimerizationProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding

2013

AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close pa…

Models MolecularStereochemistryDimerRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsCytochrome b559Sequence (biology)Context (language use)Cytochrome b559BiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundBacterial ProteinsStructural BiologyGeneticsEscherichia coliProtein Interaction Domains and MotifsAmino Acid SequenceDimerization motifMolecular Biologychemistry.chemical_classificationSequence contextHydrogen bondProtein StabilityCell MembraneMembrane ProteinsHelix–helix interactionHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinTransmembraneAmino acidTransmembrane domainchemistryDimerizationProtein BindingFEBS Letters
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Paraphyly of the Blue Tit (Parus caeruleus) suggested from cytochrome b sequences

2002

The phylogenetic relationships of the Blue Tit-Azure Tit assemblage (genus Parus; Aves: Passeriformes) were studied using mitochondrial DNA sequences of 24 specimens representing seven subspecies from Eurasia and North Africa. Previous work based on comparative morphological and acoustic data suggested a division of the Blue Tit (Parus caeruleus) into two species. Our analyses clearly indicate that the Blue Tit represents a paraphyletic assemblage, including a European/Middle Asian clade that is the sister group to the Azure Tit (Parus cyanus) and a North African clade. The North African clade (teneriffae subspecies group) is a sister group to the European Blue Tit/Azure Tit clade. We sugge…

ParaphylyAsiaZoologySubspeciesBiologyDNA MitochondrialBirdsAfrica NorthernGeneticsAnimalsCladeMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsParusLikelihood FunctionsPhylogenetic treeCytochrome bEcologyGenetic VariationCytochrome b Groupbiology.organism_classificationEuropeHaplotypesSister groupMutationMolecular phylogeneticsMolecular Phylogenetics and Evolution
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A molecular analysis of some Eastern Atlantic grouper from the Epinephelus and Mycteroperca genus

2005

Abstract Mitochondrial cytochrome b (397 bp) and 16S rDNA (516 bp) sequences analysis was used to investigate the phylogenetic relationships among some Eastern Atlantic Epinephelinae species. Six species of Epinephelus ( E. aeneus , E. caninus , E. costae , E. haifensis , E. marginatus and E. tauvina ) and two species of Mycteroperca ( M. rubra and M. fusca ) were analysed. Neighbour-joining and maximum-parsimony analysis support the paraphyletic grouping of the Epinephelus and Mycteroperca analysed. The maximum pairwise nucleotide divergence value in cyt b among all taxa was 0.196 between E. aeneus and E. marginatus and the minimum value was 0.006 between E. costae and M. rubra . Meanwhile…

ParaphylybiologyPhylogenetic treeCytochrome bEcologySettore BIO/05 - ZoologiaZoologyAquatic ScienceEpinephelusbiology.organism_classificationcyt bGenus16S rDNAGrouperMycteropercaMolecular clockPhylogenetic analysesEcology Evolution Behavior and SystematicsMycteropercaEpinepheluJournal of Experimental Marine Biology and Ecology
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Thylakoid Membrane Maturation and PSII Activation Are Linked in Greening Synechocystis sp. PCC 6803 Cells

2013

Abstract Thylakoid membranes are typical and essential features of both chloroplasts and cyanobacteria. While they are crucial for phototrophic growth of cyanobacterial cells, biogenesis of thylakoid membranes is not well understood yet. Dark-grown Synechocystis sp. PCC 6803 cells contain only rudimentary thylakoid membranes but still a relatively high amount of phycobilisomes, inactive photosystem II and active photosystem I centers. After shifting dark-grown Synechocystis sp. PCC 6803 cells into the light, “greening” of Synechocystis sp. PCC 6803 cells, i.e. thylakoid membrane formation and recovery of photosynthetic electron transport reactions, was monitored. Complete restoration of a t…

Photosystem IIPhysiologyChemistryCytochrome b6f complexfood and beveragesLight-harvesting complexes of green plantsmacromolecular substancesPlant SciencePhotosystem IBiochemistryLight-dependent reactionsThylakoidQuantasomepolycyclic compoundsGeneticsBiophysicsPhotosystemPlant Physiology
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Disentangling composite colour patterns in a poison frog species

2008

A phylogenetic approach was performed to infer whether variation in conspicuous colour-patterns of a poison frog (Dendrobatidae: Dendrobates tinctorius) has evolved neutrally or under selection. Colour and pattern were split into components that were separately analysed and subsequently re-grouped via principal component analysis. This revealed four different ‘displayed’ factors on the dorsal and lateral views versus one ‘concealed’ factor on the ventral view. Based on the assumption that current patterns of trait variation contain information about the evolutionary history of the phenotype, we correlated these trait components to a neutrally evolving gene fragment (cytochrome b). The conce…

Phylogenetic treeGenetic driftPhylogeneticsDendrobatesCytochrome bMolecular phylogeneticsZoologyDendrobatoideaAposematismBiologybiology.organism_classificationEcology Evolution Behavior and SystematicsBiological Journal of the Linnean Society
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Quality controls for cell cultures: identification of interspecies cross-contamination by PCR-RFLP analysis of the cytochrome b gene

2012

Cross-contaminations of a cell line with cells of different species represent a potential risk in laboratories handling human and animal cells. Therefore, it is necessary to control such contaminations. Tests based on mitochondrial DNA (mtDNA) are used in forensic analysis, phylogenetic studies and in food authentication. However, the use of mtDNA in quality controls of cell cultures is recent. Mitochondrial sequence differences of closely related animal species are five- to tenfold higher than those of nuclear genes. On the contrary, intraspecies variation in mitochondrial sequences is low in most animal species. Moreover, each cell contains 100–10.000 mitochondrial genomes. The amount of …

QUALITY CONTROLS CELL CULTURES INTERSPECIES CROSS-CONTAMINATION PCR-RFLP ANALYSIS CYTOCHROME B GENE
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First Data on the Molecular Phylogeography of Scincid Lizards of the Genus Mabuya

2000

A 487-bp fragment of the mitochondrial 16S rRNA gene was sequenced in 26 species of the circumtropical lizard genus Mabuya and used to analyze phylogenetic relationships within the genus. The species from Africa and Madagascar formed a monophyletic group relative to the included Asian and South American taxa. The Malagasy species included (M. elegans, M. cf. dumasi, and M. comorensis) did not appear as a monophylum. Combined and separate analysis of the 16S data and additional sequences of the mitochondrial 12S rRNA, ND4, and cytochrome b genes (a total of 2255 bp) in one Asian, two Malagasy, and two African species also did not result consistently in a monophyletic grouping of the Malagasy…

RNA MitochondrialMabuyaZoologyMonophylyGenusRNA Ribosomal 16Sbiology.animalMadagascarGeneticsAnimalsMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsbiologyPhylogenetic treeLizardCytochrome bLizardsNADH DehydrogenaseEmigration and ImmigrationCytochrome b Groupbiology.organism_classificationBiological EvolutionPhylogeographyTaxonRNA RibosomalAfricaRNAMolecular Phylogenetics and Evolution
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