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dc.contributor.authorKurttila, Moona
dc.contributor.authorStucki-Buchli, Brigitte
dc.contributor.authorRumfeldt, Jessica
dc.contributor.authorSchroeder, Lea
dc.contributor.authorHäkkänen, Heikki
dc.contributor.authorLiukkonen, Alli
dc.contributor.authorTakala, Heikki
dc.contributor.authorKottke, Tilman
dc.contributor.authorIhalainen, Janne
dc.date.accessioned2021-03-05T10:27:36Z
dc.date.available2021-03-05T10:27:36Z
dc.date.issued2021
dc.identifier.citationKurttila, M., Stucki-Buchli, B., Rumfeldt, J., Schroeder, L., Häkkänen, H., Liukkonen, A., Takala, H., Kottke, T., & Ihalainen, J. (2021). Site-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy. <i>Physical Chemistry Chemical Physics</i>, <i>23</i>(9), 5615-5628. <a href="https://doi.org/10.1039/d0cp06553f" target="_blank">https://doi.org/10.1039/d0cp06553f</a>
dc.identifier.otherCONVID_51779518
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/74502
dc.description.abstractSignal propagation in photosensory proteins is a complex and multidimensional event. Unraveling such mechanisms site-specifically in real time is an eligible but a challenging goal. Here, we elucidate the site-specific events in a red-light sensing phytochrome using the unnatural amino acid azidophenylalanine, vibrationally distinguishable from all other protein signals. In canonical phytochromes, signal transduction starts with isomerization of an excited bilin chromophore, initiating a multitude of processes in the photosensory unit of the protein, which eventually control the biochemical activity of the output domain, nanometers away from the chromophore. By implementing the label in prime protein locations and running two-color step-scan FTIR spectroscopy on the Deinococcus radiodurans bacteriophytochrome, we track the signal propagation at three specific sites in the photosensory unit. We show that a structurally switchable hairpin extension, a so-called tongue region, responds to the photoconversion already in microseconds and finalizes its structural changes concomitant with the chromophore, in milliseconds. In contrast, kinetics from the other two label positions indicate that the site-specific changes deviate from the chromophore actions, even though the labels locate in the chromophore vicinity. Several other sites for labeling resulted in impaired photoswitching, low structural stability, or no changes in the difference spectrum, which provides additional information on the inner dynamics of the photosensory unit. Our work enlightens the multidimensionality of the structural changes of proteins under action. The study also shows that the signaling mechanism of phytochromes is accessible in a time-resolved and site-specific approach by azido probes and demonstrates challenges in using these labels.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.ispartofseriesPhysical Chemistry Chemical Physics
dc.rightsCC BY-NC 3.0
dc.titleSite-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202103051862
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange5615-5628
dc.relation.issn1463-9076
dc.relation.numberinseries9
dc.relation.volume23
dc.type.versionpublishedVersion
dc.rights.copyright© the Owner Societies 2021
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber
dc.relation.grantnumber332742
dc.relation.grantnumber296135
dc.relation.grantnumber330678
dc.subject.ysofotobiologia
dc.subject.ysospektroskopia
dc.subject.ysoproteiinit
dc.subject.ysovalokemia
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p27666
jyx.subject.urihttp://www.yso.fi/onto/yso/p10176
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p7201
dc.rights.urlhttps://creativecommons.org/licenses/by-nc/3.0/
dc.relation.doi10.1039/d0cp06553f
dc.relation.funderJane and Aatos Erkko Foundationen
dc.relation.funderResearch Council of Finlanden
dc.relation.funderResearch Council of Finlanden
dc.relation.funderResearch Council of Finlanden
dc.relation.funderJane ja Aatos Erkon säätiöfi
dc.relation.funderSuomen Akatemiafi
dc.relation.funderSuomen Akatemiafi
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramFoundationen
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAcademy Research Fellow, AoFen
jyx.fundingprogramSäätiöfi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramAkatemiatutkija, SAfi
jyx.fundinginformationThe work of BS-B has been supported by a grant from the Swiss National Science Foundation (P2ZHP2_164991). JAI acknowledges the Academy of Finland (296135 and 332742) and the Jane and Aatos Erkko foundation. HT acknowledges the Academy of Finland (285461 and 330678). LS acknowledges a fellowship of the Studienstiftung des Deutschen Volkes. TK acknowledges a Heisenberg fellowship of the Deutsche Forschungsgemeinschaft (KO3580/4-2).
dc.type.okmA1


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