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Study of transport proteins of the Nramp family
dc.contributor.advisorChaloupka, Roman
dc.creatorSurá, Lucie
dc.date.accessioned2021-03-23T21:18:44Z
dc.date.available2021-03-23T21:18:44Z
dc.date.issued2009
dc.identifier.urihttp://hdl.handle.net/20.500.11956/21112
dc.description.abstractThe Natural Resistance-Associated Macrophage Proteins (Nramp) form functionally conserved family of proton-dependent divalent metal ion transporters. In the present study, we investigated transport properties of a prokaryotic Nramp homolog - MntH transporter from Escherichia coli. H+ transport mediated by MntH was monitored in a bacterial model system using pH-sensitive green fluorescent protein (pHluorin). Our experimental conditions enabled us to observe an uncoupled H+ transport mediated by MntH. Uncoupled H+ flux had been previously described in eukaryotic Nramp proteins, nevertheless this is the first observation of this phenomenon in a prokaryotic homolog. We demonstrated that the uncoupled H+ transport is pH- and temperature- dependent. The uncoupled transport H+ is also affected by specific single-point mutations at functionally important residues Asp34, His211 and Asn401. The second part of the work focused on effect of different ions, which are not MntH substrates, on transport properties of MntH. It was shown that addition of excess calcium or magnesium resulted in increase of H+ transport induced by divalent metal ions, but on the other hand our data suggest that calcium inhibits uncoupled H+ transport.en_US
dc.languageČeštinacs_CZ
dc.language.isocs_CZ
dc.publisherUniverzita Karlova, Matematicko-fyzikální fakultacs_CZ
dc.titleStudium transportních proteinů z rodiny Nrampcs_CZ
dc.typediplomová prácecs_CZ
dcterms.created2009
dcterms.dateAccepted2009-05-25
dc.description.departmentInstitute of Physics of Charles Universityen_US
dc.description.departmentFyzikální ústav UKcs_CZ
dc.description.facultyFaculty of Mathematics and Physicsen_US
dc.description.facultyMatematicko-fyzikální fakultacs_CZ
dc.identifier.repId47614
dc.title.translatedStudy of transport proteins of the Nramp familyen_US
dc.contributor.refereeHoloubek, Aleš
dc.identifier.aleph001116572
thesis.degree.nameMgr.
thesis.degree.levelnavazující magisterskécs_CZ
thesis.degree.disciplineBiophysics and Chemical Physicsen_US
thesis.degree.disciplineBiofyzika a chemická fyzikacs_CZ
thesis.degree.programPhysicsen_US
thesis.degree.programFyzikacs_CZ
uk.thesis.typediplomová prácecs_CZ
uk.taxonomy.organization-csMatematicko-fyzikální fakulta::Fyzikální ústav UKcs_CZ
uk.taxonomy.organization-enFaculty of Mathematics and Physics::Institute of Physics of Charles Universityen_US
uk.faculty-name.csMatematicko-fyzikální fakultacs_CZ
uk.faculty-name.enFaculty of Mathematics and Physicsen_US
uk.faculty-abbr.csMFFcs_CZ
uk.degree-discipline.csBiofyzika a chemická fyzikacs_CZ
uk.degree-discipline.enBiophysics and Chemical Physicsen_US
uk.degree-program.csFyzikacs_CZ
uk.degree-program.enPhysicsen_US
thesis.grade.csVýborněcs_CZ
thesis.grade.enExcellenten_US
uk.abstract.enThe Natural Resistance-Associated Macrophage Proteins (Nramp) form functionally conserved family of proton-dependent divalent metal ion transporters. In the present study, we investigated transport properties of a prokaryotic Nramp homolog - MntH transporter from Escherichia coli. H+ transport mediated by MntH was monitored in a bacterial model system using pH-sensitive green fluorescent protein (pHluorin). Our experimental conditions enabled us to observe an uncoupled H+ transport mediated by MntH. Uncoupled H+ flux had been previously described in eukaryotic Nramp proteins, nevertheless this is the first observation of this phenomenon in a prokaryotic homolog. We demonstrated that the uncoupled H+ transport is pH- and temperature- dependent. The uncoupled transport H+ is also affected by specific single-point mutations at functionally important residues Asp34, His211 and Asn401. The second part of the work focused on effect of different ions, which are not MntH substrates, on transport properties of MntH. It was shown that addition of excess calcium or magnesium resulted in increase of H+ transport induced by divalent metal ions, but on the other hand our data suggest that calcium inhibits uncoupled H+ transport.en_US
uk.file-availabilityV
uk.grantorUniverzita Karlova, Matematicko-fyzikální fakulta, Fyzikální ústav UKcs_CZ
thesis.grade.code1
dc.contributor.consultantUrbánková, Eva
uk.publication-placePrahacs_CZ
uk.thesis.defenceStatusO


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