Näytä suppeat kuvailutiedot

dc.contributor.authorWahlgren, Weixiao Yuan
dc.contributor.authorClaesson, Elin
dc.contributor.authorTuure, Iida
dc.contributor.authorTrillo-Muyo, Sergio
dc.contributor.authorBódizs, Szabolcs
dc.contributor.authorIhalainen, Janne A.
dc.contributor.authorTakala, Heikki
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2022-12-22T09:22:41Z
dc.date.available2022-12-22T09:22:41Z
dc.date.issued2022
dc.identifier.citationWahlgren, W. Y., Claesson, E., Tuure, I., Trillo-Muyo, S., Bódizs, S., Ihalainen, J. A., Takala, H., & Westenhoff, S. (2022). Structural mechanism of signal transduction in a phytochrome histidine kinase. <i>Nature Communications</i>, <i>13</i>(1), Article 7673. <a href="https://doi.org/10.1038/s41467-022-34893-3" target="_blank">https://doi.org/10.1038/s41467-022-34893-3</a>
dc.identifier.otherCONVID_164502163
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/84555
dc.description.abstractPhytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 Å and 3.5 Å resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its tertiary domain arrangement, but the connector helices between the photosensory and the histidine kinase modules open up like a zipper, causing asymmetry and disorder in the effector domains. The structures provide a framework for atom-scale understanding of signaling in phytochromes, visualize allosteric communication over several nanometers, and suggest that disorder in the dimeric arrangement of the effector domains is important for phosphatase activity in a two-component system. The results have implications for the development of optogenetic applications.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofseriesNature Communications
dc.rightsCC BY 4.0
dc.subject.otherelectron microscopy
dc.subject.otherkinases
dc.subject.otherphotochemistry
dc.subject.otherplant signalling
dc.titleStructural mechanism of signal transduction in a phytochrome histidine kinase
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202212225800
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centeren
dc.contributor.oppiaineCell and Molecular Biologyen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn2041-1723
dc.relation.numberinseries1
dc.relation.volume13
dc.type.versionpublishedVersion
dc.rights.copyright© The Author(s) 2022
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber330678
dc.relation.grantnumber332742
dc.subject.ysoelektronimikroskopia
dc.subject.ysovalokemia
dc.subject.ysokinaasit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p18917
jyx.subject.urihttp://www.yso.fi/onto/yso/p7201
jyx.subject.urihttp://www.yso.fi/onto/yso/p21135
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1038/s41467-022-34893-3
dc.relation.funderResearch Council of Finlanden
dc.relation.funderResearch Council of Finlanden
dc.relation.funderSuomen Akatemiafi
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramAcademy Research Fellow, AoFen
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAkatemiatutkija, SAfi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundinginformationS.W. acknowledges support from the European Research Council, ERC grant to Westenhoff, MolStrucDyn, 725642. This work was supported by Academy of Finland grants 332742 (J.A.I.) and 330678 (H.T.).
dc.type.okmA1


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