Clustering and Dynamics of Phototransducer Signaling Domains Revealed by Site-Directed Spin Labeling Electron Paramagnetic Resonance on SRII/HtrII in Membranes and Nanodiscs

DC FieldValueLanguage
dc.contributor.authorOrban-Glass, Ioan
dc.contributor.authorVoskoboynikova, Natalia
dc.contributor.authorBusch, Karin B.
dc.contributor.authorKlose, Daniel
dc.contributor.authorRickert, Christian
dc.contributor.authorMosslehy, Wageiha
dc.contributor.authorRoder, Friedrich
dc.contributor.authorWilkens, Verena
dc.contributor.authorPiehler, Jacob
dc.contributor.authorEngelhard, Martin
dc.contributor.authorSteinhoff, Heinz-Juergen
dc.contributor.authorKlare, Johann P.
dc.date.accessioned2021-12-23T16:08:59Z-
dc.date.available2021-12-23T16:08:59Z-
dc.date.issued2015
dc.identifier.issn00062960
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/8561-
dc.description.abstractIn halophilic archaea the photophobic response is mediated by the membrane-embedded 2:2 photoreceptor/-transducer complex SRII/HtrII, the latter being homologous to the bacterial chemoreceptors. Both systems bias the rotation direction of the flagellar motor via a two-component system coupled to an extended cytoplasmic signaling domain formed by a four helical antiparallel coiled-coil structure. For signal propagation by the HAMP domains connecting the transmembrane and cytoplasmic domains, it was suggested that a two-state thermodynamic equilibrium found for the first HAMP domain in NpSRII/NpHtrII is shifted upon activation, yet signal propagation along the coiled-coil transducer remains largely elusive, including the activation mechanism of the coupled kinase CheA. We investigated the dynamic and structural properties of the cytoplasmic tip domain of NpHtrII in terms of signal transduction and putative oligomerization using site-directed spin labeling electron paramagnetic resonance spectroscopy. We show that the cytoplasmic tip domain of NpHtrII is engaged in a two-state equilibrium between a dynamic and a compact conformation like what was found for the first HAMP domain, thus strengthening the assumption that dynamics are the language of signal transfer. Interspin distance measurements in membranes and on isolated 2:2 photoreceptor/transducer complexes in nanolipoprotein particles provide evidence that archaeal photoreceptor/-transducer complexes analogous to chemoreceptors form trimers-of-dimers or higher-order assemblies even in the absence of the cytoplasmic components CheA and CheW, underlining conservation of the overall mechanistic principles underlying archaeal phototaxis and bacterial chemotaxis systems. Furthermore, our results revealed a significant influence of the NpHtrII signaling domain on the NpSRII photocycle kinetics, providing evidence for a conformational coupling of SRII and HtrII in these complexes.
dc.description.sponsorshipVolkswagen-StiftungVolkswagen; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 944/P10, BU 2288/1-1]; Cultural Office of the Embassy of the Arab Republic of Egypt; This work was supported by the Volkswagen-Stiftung (N. V.), the Deutsche Forschungsgemeinschaft (SFB 944/P10 to J.P.K, H.-J.S. and J.P.; Grant BU 2288/1-1 to K. B.B.), and the Cultural Office of the Embassy of the Arab Republic of Egypt to W.M.
dc.language.isoen
dc.publisherAMER CHEMICAL SOC
dc.relation.ispartofBIOCHEMISTRY
dc.subjectBiochemistry & Molecular Biology
dc.subjectCROSS-CORRELATION SPECTROSCOPY
dc.subjectDIRECT VISUALIZATION
dc.subjectHAMP DOMAIN
dc.subjectMOLECULAR-BASIS
dc.subjectNATRONOBACTERIUM-PHARAONIS
dc.subjectNATRONOMONAS-PHARAONIS
dc.subjectPROTON-TRANSFER
dc.subjectRECEPTOR ARRAYS
dc.subjectSENSORY RHODOPSIN-II
dc.subjectTRANSDUCER COMPLEX
dc.titleClustering and Dynamics of Phototransducer Signaling Domains Revealed by Site-Directed Spin Labeling Electron Paramagnetic Resonance on SRII/HtrII in Membranes and Nanodiscs
dc.typejournal article
dc.identifier.doi10.1021/bi501160q
dc.identifier.isiISI:000348333300025
dc.description.volume54
dc.description.issue2
dc.description.startpage349
dc.description.endpage362
dc.contributor.orcid0000-0003-0525-0191
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-5761-5968
dc.contributor.orcid0000-0002-3597-0889
dc.contributor.researcheridABH-8594-2020
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridAAM-8374-2021
dc.contributor.researcheridC-1428-2009
dc.publisher.place1155 16TH ST, NW, WASHINGTON, DC 20036 USA
dcterms.isPartOf.abbreviationBiochemistry
dcterms.oaStatushybrid
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptSonderforschungsbereich 944: Physiologie und Dynamik zellulärer Mikrokompartimente-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.deptidfb04-
crisitem.author.deptidorganisation19-
crisitem.author.deptidfb05-
crisitem.author.deptidfb04-
crisitem.author.orcid0000-0003-2317-0144-
crisitem.author.orcid0000-0002-3597-0889-
crisitem.author.orcid0000-0002-8129-3081-
crisitem.author.orcid0000-0002-2143-2270-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgFB 05 - Biologie/Chemie-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.grandparentorgUniversität Osnabrück-
crisitem.author.netidVoNa568-
crisitem.author.netidKlDa004-
crisitem.author.netidMoWa274-
crisitem.author.netidPiJa938-
crisitem.author.netidStHe633-
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