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dc.contributor.authorTakala, Heikki
dc.contributor.authorBjörling, Alexander
dc.contributor.authorBerntsson, Oskar
dc.contributor.authorLehtivuori, Heli
dc.contributor.authorNiebling, Stephan
dc.contributor.authorHoernke, Maria
dc.contributor.authorKosheleva, Irina
dc.contributor.authorHenning, Robert
dc.contributor.authorMenzel, Andreas
dc.contributor.authorIhalainen, Janne
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2014-08-14T14:27:18Z
dc.date.available2014-10-30T22:45:04Z
dc.date.issued2014fi
dc.identifier.citationTakala, H., Björling, A., Berntsson, O., Lehtivuori, H., Niebling, S., Hoernke, M., . . . Westenhoff, S. (2014). Signal amplification and transduction in phytochrome photosensors. <em>Nature</em>, 509 (8 May), 245-248. <a href="http://dx.doi.org/10.1038/nature13310">doi:10.1038/nature13310</a>fi
dc.identifier.otherTUTKAID_62021
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/44023
dc.description.abstract[Introduction] Page 2 of 20 Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light sensing kinases that control diverse cell ular functions in plants, bacteria, and fungi. 1-9 Bacterial phytochro mes consist of a photosensory core and a C-te rminal regulatory domain. 10,11 Structures of photosensory cores are reported in the resting state 12-18 and conformational responses to light activat ion have been proposed in the vicinity of the chromophore. 19-23 However, the structure of the signalling state and the mechanism of downstream signal re lay through the photosensory core remain elusive. Here, we report crystal and solution structures of the resting and active states of the photosensory core of the bacteriophytochrome from Deinococcus radiodurans . The structures reveal an open and closed form of the dimeric protein for the signalling an d resting state, respectively. This nanometre scale rearrangement is controlled by refolding of an evolutionarily conserved “tongue” , which is in contact with the chromophore. The findings reveal an unus ual mechanism where atomic scale conformational ch anges around the chromopho re are first amplified into an Ångström scale distance change in the tongue, and further grow into a nanometre scale conformational sign al. The structural mechanism is a blueprint for understanding how the sensor proteins connect to the cellular signalling network.fi
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofseriesNature
dc.subject.othermolecular biophysicsfi
dc.subject.otherx-ray crystallographyfi
dc.subject.otherbiochemistryfi
dc.titleSignal amplification and transduction in phytochrome photosensorsfi
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201407232251
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosThe Department of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologia
dc.type.urihttp://purl.org/eprint/type/SubmittedJournalArticle
dc.date.updated2014-07-23T03:30:11Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.format.pagerange245-248
dc.relation.issn0028-0836
dc.relation.numberinseries8 May
dc.relation.volume509
dc.type.versionacceptedVersion
dc.rights.copyright© 2014 Macmillan Publishers Limited. All Rights Reserved.
dc.rights.accesslevelopenAccessfi
dc.relation.doi10.1038/nature13310


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