Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis

DC ElementWertSprache
dc.contributor.authorOrekhov, Philipp S.
dc.contributor.authorKlose, Daniel
dc.contributor.authorMulkidjanian, Armen Y.
dc.contributor.authorShaitan, Konstantin V.
dc.contributor.authorEngelhard, Martin
dc.contributor.authorKlare, Johann P.
dc.contributor.authorSteinhoff, Heinz-Juergen
dc.date.accessioned2021-12-23T16:14:49Z-
dc.date.available2021-12-23T16:14:49Z-
dc.date.issued2015
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11265-
dc.description.abstractMotile 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.sponsorshipDeutsche 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.isoen
dc.publisherPUBLIC LIBRARY SCIENCE
dc.relation.ispartofPLOS COMPUTATIONAL BIOLOGY
dc.subjectASPARTATE RECEPTOR
dc.subjectBACILLUS-SUBTILIS CHEMOTAXIS
dc.subjectBiochemical Research Methods
dc.subjectBiochemistry & Molecular Biology
dc.subjectCYTOPLASMIC DOMAIN
dc.subjectFORCE-FIELD
dc.subjectHAMP DOMAIN
dc.subjectHELIX ROTATION
dc.subjectMathematical & Computational Biology
dc.subjectMETHYLATION SITES
dc.subjectMUTATIONAL ANALYSIS
dc.subjectSENSORY-RHODOPSIN-II
dc.subjectSTRUCTURAL DETERMINANTS
dc.titleSignaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis
dc.typejournal article
dc.identifier.doi10.1371/journal.pcbi.1004561
dc.identifier.isiISI:000364399700080
dc.description.volume11
dc.description.issue10
dc.contributor.orcid0000-0002-5761-5968
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0003-4078-4762
dc.contributor.orcid0000-0001-5844-3064
dc.contributor.orcid0000-0002-3597-0889
dc.contributor.researcheridC-1428-2009
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridV-5214-2017
dc.contributor.researcheridJ-8086-2013
dc.contributor.researcheridAAH-3608-2021
dc.identifier.eissn15537358
dc.publisher.place1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
dcterms.isPartOf.abbreviationPLoS Comput. Biol.
dcterms.oaStatusGreen Published, Green Submitted, gold
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptUniversität Osnabrück-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.deptidfb04-
crisitem.author.orcid0000-0002-3597-0889-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidKlDa004-
crisitem.author.netidShKo001-
crisitem.author.netidStHe633-
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