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dc.contributor.authorMultamäki, Elina
dc.contributor.authorNanekar, Rahul
dc.contributor.authorMorozov, Dmitry
dc.contributor.authorLievonen, Topias
dc.contributor.authorGolonka, David
dc.contributor.authorWahlgren, Weixiao Yuan
dc.contributor.authorStucki-Buchli, Brigitte
dc.contributor.authorRossi, Jari
dc.contributor.authorHytönen, Vesa P.
dc.contributor.authorWestenhoff, Sebastian
dc.contributor.authorIhalainen, Janne A.
dc.contributor.authorMöglich, Andreas
dc.contributor.authorTakala, Heikki
dc.date.accessioned2021-07-27T07:38:39Z
dc.date.available2021-07-27T07:38:39Z
dc.date.issued2021
dc.identifier.citationMultamäki, E., Nanekar, R., Morozov, D., Lievonen, T., Golonka, D., Wahlgren, W. Y., Stucki-Buchli, B., Rossi, J., Hytönen, V. P., Westenhoff, S., Ihalainen, J. A., Möglich, A., & Takala, H. (2021). Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling. <i>Nature Communications</i>, <i>12</i>, Article 4394. <a href="https://doi.org/10.1038/s41467-021-24676-7" target="_blank">https://doi.org/10.1038/s41467-021-24676-7</a>
dc.identifier.otherCONVID_99079024
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/77214
dc.description.abstractBacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP as a light-sensitive phosphatase. While Agp1 binds its cognate response regulator only transiently, DrBphP does so strongly, which is rationalized at the structural level. Our data pinpoint two key residues affecting the balance between kinase and phosphatase activities, which immediately bears on photoreception and two-component signaling. The opposing output activities in two highly similar bacteriophytochromes suggest the use of light-controllable histidine kinases and phosphatases for optogenetics.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherSpringer Science and Business Media LLC
dc.relation.ispartofseriesNature Communications
dc.rightsCC BY 4.0
dc.subject.otherbacterial phytochromes
dc.subject.otherphotoreceptors
dc.titleComparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202107274386
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineFysikaalinen kemiafi
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centeren
dc.contributor.oppiainePhysical Chemistryen
dc.contributor.oppiaineCell and Molecular Biologyen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.description.reviewstatuspeerReviewed
dc.relation.issn2041-1723
dc.relation.volume12
dc.type.versionpublishedVersion
dc.rights.copyright© The Author(s) 2021
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber330678
dc.relation.grantnumber823830
dc.relation.grantnumber823830
dc.relation.grantnumber332742
dc.relation.grantnumber296135
dc.relation.grantnumber
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/H2020/823830/EU//BioExcel-2
dc.format.contentfulltext
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1038/s41467-021-24676-7
dc.relation.funderSuomen Akatemiafi
dc.relation.funderEuroopan komissiofi
dc.relation.funderSuomen Akatemiafi
dc.relation.funderSuomen Akatemiafi
dc.relation.funderJane ja Aatos Erkon säätiöfi
dc.relation.funderAcademy of Finlanden
dc.relation.funderEuropean Commissionen
dc.relation.funderAcademy of Finlanden
dc.relation.funderAcademy of Finlanden
dc.relation.funderJane and Aatos Erkko Foundationen
jyx.fundingprogramAkatemiatutkijan tehtävä, SAfi
jyx.fundingprogramResearch infrastructures, H2020fi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramSäätiöfi
jyx.fundingprogramResearch post as Academy Research Fellow, AoFen
jyx.fundingprogramResearch infrastructures, H2020en
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramFoundationen
jyx.fundinginformationThis work was supported by Academy of Finland grants 285461, 330678 (H.T.), 296135, and 332742 (J.A.I.), Jane and Aatos Erkko Foundation (J.A.I.), Three-year grant 2018–2020 from the University of Helsinki (E.M. and H.T.), and Bayreuth Humboldt Centre Senior Fellowship 2020 (E.M. and H.T.). S.W. and W.W. acknowledge the European Research Council for support (grant number: 279944), and B.S.-B. acknowledges Swiss National Science Foundation (P2ZHP2_164991). D.M. acknowledge the BioExcel CoE (www.bioexcel.eu), funded by the European Union contracts H2020-INFRAEDI-02-2018-823830, H2020-EINFRA-2015-1-675728.


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