Site-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy
Kurttila, 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. Physical Chemistry Chemical Physics, 23(9), 5615-5628. https://doi.org/10.1039/d0cp06553f
Julkaistu sarjassa
Physical Chemistry Chemical PhysicsTekijät
Päivämäärä
2021Tekijänoikeudet
© the Owner Societies 2021
Signal 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.
...
Julkaisija
Royal Society of Chemistry (RSC)ISSN Hae Julkaisufoorumista
1463-9076Asiasanat
Julkaisu tutkimustietojärjestelmässä
https://converis.jyu.fi/converis/portal/detail/Publication/51779518
Metadata
Näytä kaikki kuvailutiedotKokoelmat
Rahoittaja(t)
Jane ja Aatos Erkon säätiö; Suomen AkatemiaRahoitusohjelmat(t)
Säätiö; Akatemiahanke, SA; Akatemiatutkija, SALisätietoja rahoituksesta
The 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). ...Lisenssi
Samankaltainen aineisto
Näytetään aineistoja, joilla on samankaltainen nimeke tai asiasanat.
-
Tips and turns of bacteriophytochrome photoactivation
Takala, Heikki; Edlund, Petra; Ihalainen, Janne A.; Westenhoff, Sebastian (Royal Society of Chemistry (RSC), 2020)Phytochromes 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. ... -
Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome
Lehtivuori, Heli; Rumfeldt, Jessica; Mustalahti, Satu; Kurkinen, Sami; Takala, Heikki (Springer Science and Business Media LLC, 2022)Phytochromes are red light-sensing photoreceptor proteins that bind a bilin chromophore. Here, we investigate the role of a conserved histidine (H260) and tyrosine (Y263) in the chromophore-binding domain (CBD) of Deinococcus ... -
Structural mechanism of signal transduction in a phytochrome histidine kinase
Wahlgren, Weixiao Yuan; Claesson, Elin; Tuure, Iida; Trillo-Muyo, Sergio; Bódizs, Szabolcs; Ihalainen, Janne A.; Takala, Heikki; Westenhoff, Sebastian (Nature Publishing Group, 2022)Phytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory ... -
Coordination of the biliverdin D-ring in bacteriophytochromes
Lenngren, Nils; Edlund, Petra; Takala, Heikki; Stucki-Buchli, Brigitte; Rumfeldt, Jessica; Peshev, Ivan; Häkkänen, Heikki; Westenhoff, Sebastian; Ihalainen, Janne (Royal Society of Chemistry, 2018)Phytochrome proteins translate light into biochemical signals in plants, fungi and microorganisms. Light cues are absorbed by a bilin chromophore, leading to an isomerization and a rotation of the D-ring. This relays the ... -
Protonation of the Biliverdin IXα Chromophore in the Red and Far-Red Photoactive States of Bacteriophytochrome
Modi, Vaibhav; Donnini, Serena; Groenhof, Gerrit; Morozov, Dmitry (American Chemical Society, 2019)The tetrapyrrole chromophore biliverdin IXα (BV) in the bacteriophytochrome from Deinococcus radiodurans (DrBphP) is usually assumed to be fully protonated, but this assumption has not been systematically validated by ...
Ellei toisin mainittu, julkisesti saatavilla olevia JYX-metatietoja (poislukien tiivistelmät) saa vapaasti uudelleenkäyttää CC0-lisenssillä.