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dc.contributor.advisorIhalainen,Janne
dc.contributor.authorXie, Sisi
dc.date.accessioned2015-12-09T09:06:34Z
dc.date.available2015-12-09T09:06:34Z
dc.date.issued2015
dc.identifier.otheroai:jykdok.linneanet.fi:1505532
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/48030
dc.description.abstractPhytochromes are bimodal light switchable photosensors exist in plants, bacteria and fungi. Incorporating bilin as their chromophore, most bacteriophytochromes (BphPs) function as two-component histidine kinase affected by red/far-red light and regulate downstream physiological activities in the microorganism. The study aims on the purification of Agrobacterium phytochrome Agp1whose phosphorylation activity in its histidine kinase (HK) domain was recently found to be affected by the temperature. The purified proteins Agp1 were assembled with biliverdin IXα (BV) and monitored by UV-vis spectroscopy with BV incorporated DrBphP from Deinococcus radiodurans. Extinction coefficient spectra of “absolute” Pr and Pfr state of Agp1 together with free BV were drawn. The UV spectra and difference spectra of Agp1 and DrBphP were compared and band assignments were made. According to the evaluation of absorption maximum (λmax) and extinction coefficiency (Ɛ), the near blue region band at 314-320 nm in the difference spectra was assigned to tyrosine absorption. Further analysis of the band assignment and structure of Agp1 and DrBphP reveal that the 314-320 nm band is caused by the interaction of B ring propionate side chain of incorporated chromophore BV with neighboring conserved Tyr216 and/or the D ring carbonyl group with Tyr176 residues. The discovery was evidenced by the literature evaluation of the spectra of tyrosine mutants from BphPs and Synechocystis sp. Cph1. Chromophore and tyrosine interaction as a possible signaling way of BphPs was discussed based on the assignment.en
dc.format.extent1 verkkoaineisto (48 sivua)
dc.language.isoeng
dc.rightsJulkaisu on tekijänoikeussäännösten alainen. Teosta voi lukea ja tulostaa henkilökohtaista käyttöä varten. Käyttö kaupallisiin tarkoituksiin on kielletty.fi
dc.rightsThis publication is copyrighted. You may download, display and print it for Your own personal use. Commercial use is prohibited.en
dc.subject.otherfytokromi
dc.titleProtein purification of Agrobacterium tumefaciens phytochrome Agp1 and UV-vis spectroscopy analysis in comparison to DrBphP from Deinococcus Radiodurans
dc.identifier.urnURN:NBN:fi:jyu-201512093943
dc.type.ontasotPro gradufi
dc.type.ontasotMaster's thesisen
dc.contributor.tiedekuntaMatemaattis-luonnontieteellinen tiedekuntafi
dc.contributor.tiedekuntaFaculty of Sciencesen
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.yliopistoUniversity of Jyväskyläen
dc.contributor.yliopistoJyväskylän yliopistofi
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineCell and molecular biologyen
dc.date.updated2015-12-09T09:06:35Z
dc.rights.accesslevelopenAccessfi
dc.contributor.oppiainekoodi4013
dc.subject.ysosolubiologia
dc.subject.ysopuhdistus
dc.subject.ysospektroskopia
dc.subject.ysotyrosiini
dc.subject.ysoaminohapot
dc.subject.ysoimeytyminen


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