Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers
DC Element | Wert | Sprache |
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dc.contributor.author | Orekhov, Philipp | |
dc.contributor.author | Bothe, Arne | |
dc.contributor.author | Steinhoff, Heinz-Juergen | |
dc.contributor.author | Shaitan, Konstantin V. | |
dc.contributor.author | Raunser, Stefan | |
dc.contributor.author | Fotiadis, Dimitrios | |
dc.contributor.author | Schlesinger, Ramona | |
dc.contributor.author | Klare, Johann P. | |
dc.contributor.author | Engelhard, Martin | |
dc.date.accessioned | 2021-12-23T16:22:10Z | - |
dc.date.available | 2021-12-23T16:22:10Z | - |
dc.date.issued | 2017 | |
dc.identifier.issn | 00318655 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14192 | - |
dc.description.abstract | Archaeal photoreceptors consist of sensory rhodopsins in complex with their cognate transducers. After light excitation, a two-component signaling chain is activated, which is homologous to the chemotactic signaling cascades in enterobacteria. The latter system has been studied in detail. From structural and functional studies, a picture emerges which includes stable signaling complexes, which assemble to receptor arrays displaying hexagonal structural elements. At this higher order structural level, signal amplification and sensory adaptation occur. Here, we describe electron microscopy data, which show that also the archaeal phototaxis receptors sensory rhodopsin I and II in complex with their cognate transducers can form hexagonal lattices even in the presence of a detergent. This result could be confirmed by molecular dynamics calculations, which revealed similar structural elements. Calculations of the global modes of motion displayed one mode, which resembles the U-V transition of the NpSRII:NpHtrII complex, which was previously argued to represent a functionally relevant global conformational change accompanying the activation process [Ishchenko et al. (2013) J. Photochem. Photobiol. B 123, 55-58]. A model of cooperativity at the transmembrane level is discussed. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB944, P10]; DAAD program ``Ostpartnerschaften''; Ministry of Education and Science of the Russian FederationMinistry of Education and Science, Russian Federation [RFMEEI61615X0044]; Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [17-04-01219]; This work has been supported by the Deutsche Forschungsgemeinschaft (SFB944, P10 to HJS), by the DAAD program ``Ostpartnerschaften'', by the Ministry of Education and Science of the Russian Federation (RFMEEI61615X0044), and by the Russian Foundation for Basic Research (RFBR, grant 17-04-01219). Computational facilities of the Lomonosov Supercomputing Center of Moscow State University were used. We thank Rouslan Efremov and Christos Gatsogiannis for initial advice and discussion about the EM-experiments and Ramona Justinger (Forschungszentrum Julich) for excellent technical support. | |
dc.language.iso | en | |
dc.publisher | WILEY | |
dc.relation.ispartof | PHOTOCHEMISTRY AND PHOTOBIOLOGY | |
dc.subject | BACTERIAL CHEMOSENSORY ARRAY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Biophysics | |
dc.subject | CHEA KINASE | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | FUNCTIONAL EXPRESSION | |
dc.subject | GENE FUSION | |
dc.subject | HALOBACTERIAL TRANSDUCER | |
dc.subject | METHYL-ACCEPTING PROTEIN | |
dc.subject | PHARAONIS PHOBORHODOPSIN | |
dc.subject | SIGNAL-TRANSDUCTION | |
dc.subject | STRUCTURAL DETERMINANTS | |
dc.title | Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers | |
dc.type | journal article | |
dc.identifier.doi | 10.1111/php.12763 | |
dc.identifier.isi | ISI:000401262000018 | |
dc.description.volume | 93 | |
dc.description.issue | 3 | |
dc.description.startpage | 796 | |
dc.description.endpage | 804 | |
dc.contributor.orcid | 0000-0002-7716-4439 | |
dc.contributor.orcid | 0000-0002-5888-0157 | |
dc.contributor.orcid | 0000-0002-5761-5968 | |
dc.contributor.orcid | 0000-0003-4078-4762 | |
dc.contributor.orcid | 0000-0001-9373-3016 | |
dc.contributor.researcherid | W-2620-2018 | |
dc.contributor.researcherid | H-3791-2014 | |
dc.contributor.researcherid | C-1428-2009 | |
dc.contributor.researcherid | V-5214-2017 | |
dc.identifier.eissn | 17511097 | |
dc.publisher.place | 111 RIVER ST, HOBOKEN 07030-5774, NJ USA | |
dcterms.isPartOf.abbreviation | Photochem. Photobiol. | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.dept | Universität Osnabrück | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |
crisitem.author.netid | ShKo001 | - |
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