Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis
DC Element | Wert | Sprache |
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dc.contributor.author | Orekhov, Philipp S. | |
dc.contributor.author | Klose, Daniel | |
dc.contributor.author | Mulkidjanian, Armen Y. | |
dc.contributor.author | Shaitan, Konstantin V. | |
dc.contributor.author | Engelhard, Martin | |
dc.contributor.author | Klare, Johann P. | |
dc.contributor.author | Steinhoff, Heinz-Juergen | |
dc.date.accessioned | 2021-12-23T16:14:49Z | - |
dc.date.available | 2021-12-23T16:14:49Z | - |
dc.date.issued | 2015 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/11265 | - |
dc.description.abstract | Motile bacteria and archaea respond to chemical and physical stimuli seeking optimal conditions for survival. To this end transmembrane chemo- and photoreceptors organized in large arrays initiate signaling cascades and ultimately regulate the rotation of flagellar motors. To unravel the molecular mechanism of signaling in an archaeal phototaxis complex we performed coarse-grained molecular dynamics simulations of a trimer of receptor/transducer dimers, namely NpSRII/NpHtrII from Natronomonas pharaonis. Signaling is regulated by a reversible methylation mechanism called adaptation, which also influences the level of basal receptor activation. Mimicking two extreme methylation states in our simulations we found conformational changes for the transmembrane region of NpSRII/NpHtrII which resemble experimentally observed light-induced changes. Further downstream in the cytoplasmic domain of the transducer the signal propagates via distinct changes in the dynamics of HAMP1, HAMP2, the adaptation domain and the binding region for the kinase CheA, where conformational rearrangements were found to be subtle. Overall these observations suggest a signaling mechanism based on dynamic allostery resembling models previously proposed for E. coli chemoreceptors, indicating similar properties of signal transduction for archaeal photoreceptors and bacterial chemoreceptors. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 944]; Deutscher Akademischer AustauschdienstDeutscher Akademischer Austausch Dienst (DAAD); This work was supported by the Deutsche Forschungsgemeinschaft (SFB 944) (HJS) and by the Deutscher Akademischer Austauschdienst (HJS). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. | |
dc.language.iso | en | |
dc.publisher | PUBLIC LIBRARY SCIENCE | |
dc.relation.ispartof | PLOS COMPUTATIONAL BIOLOGY | |
dc.subject | ASPARTATE RECEPTOR | |
dc.subject | BACILLUS-SUBTILIS CHEMOTAXIS | |
dc.subject | Biochemical Research Methods | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CYTOPLASMIC DOMAIN | |
dc.subject | FORCE-FIELD | |
dc.subject | HAMP DOMAIN | |
dc.subject | HELIX ROTATION | |
dc.subject | Mathematical & Computational Biology | |
dc.subject | METHYLATION SITES | |
dc.subject | MUTATIONAL ANALYSIS | |
dc.subject | SENSORY-RHODOPSIN-II | |
dc.subject | STRUCTURAL DETERMINANTS | |
dc.title | Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis | |
dc.type | journal article | |
dc.identifier.doi | 10.1371/journal.pcbi.1004561 | |
dc.identifier.isi | ISI:000364399700080 | |
dc.description.volume | 11 | |
dc.description.issue | 10 | |
dc.contributor.orcid | 0000-0002-5761-5968 | |
dc.contributor.orcid | 0000-0002-5888-0157 | |
dc.contributor.orcid | 0000-0003-4078-4762 | |
dc.contributor.orcid | 0000-0001-5844-3064 | |
dc.contributor.orcid | 0000-0002-3597-0889 | |
dc.contributor.researcherid | C-1428-2009 | |
dc.contributor.researcherid | H-3791-2014 | |
dc.contributor.researcherid | V-5214-2017 | |
dc.contributor.researcherid | J-8086-2013 | |
dc.contributor.researcherid | AAH-3608-2021 | |
dc.identifier.eissn | 15537358 | |
dc.publisher.place | 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA | |
dcterms.isPartOf.abbreviation | PLoS Comput. Biol. | |
dcterms.oaStatus | Green Published, Green Submitted, gold | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.dept | Universität Osnabrück | - |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.orcid | 0000-0002-3597-0889 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | KlDa004 | - |
crisitem.author.netid | ShKo001 | - |
crisitem.author.netid | StHe633 | - |
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