Search results for "transmembrane domain"

showing 10 items of 99 documents

Vanillin cell sensor

2007

Our project for iGEM 2006 consisted of designing a cellular vanillin biosensor. We used an EnvZ -E. coli strain as a chassis, and constructed two different devices: a sensor and an actuator, assembled using OmpR-P as a standardised mediator. The sensor device contained a computation- ally designed vanillin receptor and a synthetic two-component signal transduction protein (Trz). The receptor protein was based on a ribose-binding protein as scaffold. The Trz was built by fusion of the periplasmic and transmembrane domains of a Trg protein with an EnvZ kinase domain. When the receptor complex binds Trg, an allosteric motion is propagated to the cyto- plasmic EnvZ kinase domain, resulting in a…

0303 health sciencesReceptor complex030303 biophysicsAllosteric regulationAutophosphorylationBioengineeringCell BiologyBiologyCell biology03 medical and health sciencesSynthetic biologyTransmembrane domainProtein kinase domainBiochemistry[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologySignal transductionMolecular BiologyTranscription factor030304 developmental biologyBiotechnologyIET Synthetic Biology
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Characterizing BCL-2 family protein domains in membranes:insertion, interaction and apoptotic modulation roles

2015

El objetivo de mi tesis doctoral es el estudio de los dominios transmembrana (TMD) de las proteínas de la familia Bcl-2. La principal función de esta familia de proteínas es la regulación del proceso apoptótico (1,2). Para Ello, se establece un balance de interacciones proteína-proteína entre los miembros pro- y antiapoptóticos de esta familia proteica (3,4). Nuestra hipótesis de trabajo postula que los fragmentos transmembrana de dichas proteínas pueden estar implicados no sólo en su localización subcelular sino también en el establecimiento de la red de interacciones entre proteínas Bcl-2 así como en el desarrollo de su función apoptótica.. Para corroborar esta hipótesis, hemos analizado …

230299bcl-2apoptosiscancertransmembrane domain
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Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain

2021

Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating and/or stabilizing transmembrane helix oligomers remains mostly elusive. Yet, the mere existence of (small)xxx(small) motifs in transmembrane helices is frequently used to model dimeric TM helix structures. The single transmembrane helix of the human carbonic anhydrases XII contains a large number of amino acids with small side chains, and critical involvement of these small amino acids in dimerization of the transmembrane domain has been sugges…

540 Chemistry and allied sciencesGALLEXGxxxGChemical technologycarbonic anhydrase XIITP1-1185transmembrane domainArticle570 Life sciencessmall amino acidsChemical engineering540 ChemieTP155-156interaction propensity570 Biowissenschaftenhelix–helix interactioninteraction motifMembranes
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Identification of two novel polymorphisms and a rare deletion variant in the human dopamine D4 receptor gene

1995

We report two novel polymorphisms and a rare deletion variant in the human dopaine D4 receptor gene. The two polymorphisms are characterized by single base pair substitutions, namely a G-->C transversion changing codon 11 from GGG (encoding Gly) to CGG (encoding Arg) and a C-->T transition in position -11 upstream from the start codon. The Arg11 variant occurs at a frequency of about 1% and the C-->T transition at a frequency of about 7% in German control subjects (n = 148). Allele frequencies observed in patients suffering from schizophrenia (n = 256) and bipolar affective disorder (n = 99) were similar. The deletion variant is characterized by a 21 bp deletion affecting codons 36 to 42 co…

AdultObsessive-Compulsive DisorderBipolar DisorderMolecular Sequence DataBiologymedicine.disease_causePolymerase Chain ReactionGene FrequencyStart codonReference ValuesLeukocytesGeneticsmedicineHumansPoint MutationAmino Acid SequenceAge of OnsetCodonTransversionGeneAllele frequencyBiological PsychiatryGenetics (clinical)DNA PrimersRepetitive Sequences Nucleic AcidSequence DeletionGeneticsMutationBase SequenceTransition (genetics)Receptors Dopamine D2Receptors Dopamine D4Genetic VariationDNAExonsMiddle Agedmedicine.diseasePsychiatry and Mental healthTransmembrane domainSchizophreniaSchizophreniaPanic DisorderPolymorphism Restriction Fragment Length
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Differential cysteine depletion in respiratory chain complexes enables the distinction of longevity from aerobicity.

2010

Mitochondrially encoded proteins in long-lived animals exhibit a characteristic anomaly on the amino acid usage level: they abstain from the use of cysteine in a lifespan-dependent fashion. Here, we have further investigated this phenomenon by analyzing respiratory chain complex subunits individually. We find that complex I cysteine depletion is the almost exclusive carrier of the cysteine-lifespan correlation, whereas complex IV cysteine depletion is uniform in all aerobic animals, unrelated to longevity, but even more pronounced than complex I cysteine depletion in the longest-lived species. In nuclear encoded subunits of the respiratory chain, we find lifespan-independent cysteine deplet…

AgingTime FactorsProtein ConformationRespiratory chainBiologyProtein oxidationProtein Structure SecondaryElectron TransportProtein structureOxygen ConsumptionAnimalsHumansCysteineSulfhydryl CompoundsPhylogenychemistry.chemical_classificationCell NucleusRespiratory chain complexMembrane ProteinsAerobiosisAmino acidMitochondriaProtein Structure TertiaryTransmembrane domainOxidative StressBiochemistrychemistryMembrane proteinDevelopmental BiologyCysteineMechanisms of ageing and development
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Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins

2004

For functional diversity, the large (L) envelope protein of hepatitis B virus (HBV) acquires a dual transmembrane topology via co-translational membrane integration of the S region and partial post-translational translocation of the preS subdomain. Because each process requires the second transmembrane segment (TM2), we explored the action of this determinant by using protease protection analysis of mutant L proteins. We demonstrated that neither the disruption of a leucine zipper-like motif by multiple alanine substitutions nor the flanking charges of TM2 affected the topological reorientation of L. The dispensability of both putative subunit interaction modules argues against a link betwe…

AlanineHepatitis B virusHepatitis B virusVirus AssemblyAmino Acid MotifsMolecular Sequence DataProtein domainPhenotype mixingBiological TransportBiologyEndoplasmic Reticulummedicine.disease_causeVirologyTransmembrane domainDual topologyAmino Acid SubstitutionViral Envelope ProteinsVirologyMembrane topologymedicineHepadnavirusAmino Acid SequenceProtein Processing Post-TranslationalJournal of General Virology
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Dissection of the relative contribution of the Schizosaccharomyces pombe Ctr4 and Ctr5 proteins to the copper transport and cell surface delivery fun…

2011

The Ctr1 family of proteins mediates high-affinity copper (Cu) acquisition in eukaryotic organisms. In the fission yeastSchizosaccharomyces pombe, Cu uptake is carried out by a heteromeric complex formed by the Ctr4 and Ctr5 proteins. Unlike human andSaccharomyces cerevisiaeCtr1 proteins, Ctr4 and Ctr5 are unable to function independently in Cu acquisition. Instead, both proteins physically interact with each other to form a Ctr4–Ctr5 heteromeric complex, and are interdependent for secretion to the plasma membrane and Cu transport activity. In this study, we usedS. cerevisiaemutants that are defective in high-affinity Cu uptake to dissect the relative contribution of Ctr4 and Ctr5 to the Cu…

Amino Acid MotifsMutantSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologyMicrobiologySchizosaccharomycesHumansSecretionAmino Acid SequenceSLC31 ProteinsCation Transport ProteinsCell MembraneGenetic Complementation Testbiology.organism_classificationFusion proteinYeastProtein Structure TertiaryCell biologyComplementationTransmembrane domainBiochemistryCell and Molecular Biology of MicrobesSchizosaccharomyces pombeSchizosaccharomyces pombe ProteinsSequence AlignmentCopper
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Interaction of theEscherichia colitransporter DctA with the sensor kinase DcuS: presence of functional DctA/DcuS sensor units

2012

The aerobic Escherichia coli C(4) -dicarboxylate transporter DctA and the anaerobic fumarate/succinate antiporter DcuB function as obligate co-sensors of the fumarate responsive sensor kinase DcuS under aerobic or anaerobic conditions respectively. Overproduction under anaerobic conditions allowed DctA to replace DcuB in co-sensing, indicating their functional equivalence in this capacity. In vivo interaction studies between DctA and DcuS using FRET or a bacterial two-hybrid system (BACTH) demonstrated their interaction. DctA-YFP bound to an affinity column and was able to retain DcuS. DctA shows substantial sequence and secondary structure conservation to Glt(Ph), the Na(+)/glutamate sympo…

AntiporterPlasma protein bindingBiologybiology.organism_classificationmedicine.disease_causeMicrobiologyPyrococcus horikoshiiTransmembrane domainBiochemistryHelixSymportermedicineMolecular BiologyEscherichia coliProtein secondary structureMolecular Microbiology
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Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments

2012

Abstract Hydrophobic mismatch still represents a puzzle for transmembrane peptides, despite the apparent simplicity of this concept and its demonstrated validity in natural membranes. Using a wealth of available experimental 2 H NMR data, we provide here a comprehensive explanation of the orientation and dynamics of model peptides in lipid bilayers, which shows how they can adapt to membranes of different thickness. The orientational adjustment of transmembrane α-helices can be understood as the result of a competition between the thermodynamically unfavorable lipid repacking associated with peptide tilting and the optimization of peptide/membrane hydrophobic coupling. In the positive misma…

BiophysicsAnchoringPeptideBiochemistryProtein Structure SecondaryHydrophobic mismatchXWALP peptide familyDynamics of transmembrane peptidesOrientation of transmembrane peptidesWALP peptide familyLipid bilayerPeptide sequencechemistry.chemical_classificationCell MembraneMembrane ProteinsCell BiologyTransmembrane proteinCrystallographyTransmembrane domainMembranechemistryModels ChemicalBiophysicsHydrophobic and Hydrophilic InteractionsPeptide tilt angleSolid-state 2H NMRBiochimica et Biophysica Acta (BBA) - Biomembranes
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Membrane topology of gp41 and amyloid precursor protein: Interfering transmembrane interactions as potential targets for HIV and Alzheimer treatment

2009

AbstractThe amyloid precursor protein (APP), that plays a critical role in the development of senile plaques in Alzheimer disease (AD), and the gp41 envelope protein of the human immunodeficiency virus (HIV), the causative agent of the acquired immunodeficiency syndrome (AIDS), are single-spanning type-1 transmembrane (TM) glycoproteins with the ability to form homo-oligomers. In this review we describe similarities, both in structural terms and sequence determinants of their TM and juxtamembrane regions. The TM domains are essential not only for anchoring the proteins in membranes but also have functional roles. Both TM segments contain GxxxG motifs that drive TM associations within the li…

BiophysicsHIV InfectionsBiologyGp41BiochemistryArticleTransmembrane segmentAmyloid beta-Protein PrecursorMembranes (Biologia)Alzheimer DiseaseAmyloid precursor proteinAnimalsHumansSenile plaqueschemistry.chemical_classificationCell MembraneMembraneHIVCell Biologygp41HIV Envelope Protein gp41Transmembrane proteinVirusCell biologyTransmembrane domainchemistryBiochemistryAmyloid precursor proteinMembrane topologyAlzheimerHIV-1biology.proteinGlycoproteinSequence motifBiochimica et Biophysica Acta (BBA) - Biomembranes
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