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dc.contributor.authorTakala, Heikki
dc.contributor.authorEdlund, Petra
dc.contributor.authorIhalainen, Janne A.
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2020-10-30T10:07:38Z
dc.date.available2020-10-30T10:07:38Z
dc.date.issued2020
dc.identifier.citationTakala, H., Edlund, P., Ihalainen, J. A., & Westenhoff, S. (2020). Tips and turns of bacteriophytochrome photoactivation. <i>Photochemical and Photobiological Sciences</i>, <i>19</i>(11), 1488-1510. <a href="https://doi.org/10.1039/D0PP00117A" target="_blank">https://doi.org/10.1039/D0PP00117A</a>
dc.identifier.otherCONVID_43407675
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/72404
dc.description.abstractPhytochromes are ubiquitous photosensor proteins, which control the growth, reproduction and movement in plants, fungi and bacteria. Phytochromes switch between two photophysical states depending on the light conditions. In analogy to molecular machines, light absorption induces a series of structural changes that are transduced from the bilin chromophore, through the protein, and to the output domains. Recent progress towards understanding this structural mechanism of signal transduction has been manifold. We describe this progress with a focus on bacteriophytochromes. We describe the mechanism along three structural tiers, which are the chromophore-binding pocket, the photosensory module, and the output domains. We discuss possible interconnections between the tiers and conclude by presenting future directions and open questions. We hope that this review may serve as a compendium to guide future structural and spectroscopic studies designed to understand structural signaling in phytochromes.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.ispartofseriesPhotochemical and Photobiological Sciences
dc.rightsCC BY-NC 4.0
dc.subject.otherbacteriophytochrome photoactivation
dc.titleTips and turns of bacteriophytochrome photoactivation
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202010306449
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.description.reviewstatuspeerReviewed
dc.format.pagerange1488-1510
dc.relation.issn1474-905X
dc.relation.numberinseries11
dc.relation.volume19
dc.type.versionpublishedVersion
dc.rights.copyright© The Royal Society of Chemistry and Owner Societies 2020
dc.rights.accesslevelopenAccessfi
dc.subject.ysovalokemia
dc.subject.ysobakteerit
dc.subject.ysoproteiinit
dc.subject.ysofotobiologia
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p7201
jyx.subject.urihttp://www.yso.fi/onto/yso/p1749
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p27666
dc.rights.urlhttps://creativecommons.org/licenses/by-nc/4.0/
dc.relation.doi10.1039/D0PP00117A


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