Light-induced structural changes in a full-length cyanobacterial phytochrome probed by time-resolved X-ray scattering

Derren Heyes, Samantha Hardman, Martin N Pedersen, Joyce Woodhouse, Eugenio De La Mora, Michael Wulff, Martin Weik, Marco Cammarata, Nigel Scrutton, Giorgio Schiro

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Phytochromes are photoreceptor proteins that transmit a light signal from a photosensory region to an output domain. Photoconversion involves protein conformational changes whose nature is not fully understood. Here, we use time-resolved X-ray scattering and optical spectroscopy to study the kinetics of structural changes in a full-length cyanobacterial phytochrome and in a truncated form with no output domain. X-ray and spectroscopic signals on the µs/ms timescale are largely independent of the presence of the output domain. On longer time-scales, large differences between the full-length and truncated proteins indicate the timeframe during which the structural transition is transmitted from the photosensory region to the output domain and represent a large quaternary motion. The suggested independence of the photosensory-region dynamics on the µs/ms timescale defines a time window in which the photoreaction can be characterized (e.g. for optogenetic design) independently of the nature of the engineered output domain.
    Original languageEnglish
    JournalCommunications Biology
    Volume2
    Issue number1
    Early online date3 Jan 2019
    DOIs
    Publication statusPublished - 2019

    Research Beacons, Institutes and Platforms

    • Manchester Institute of Biotechnology

    Fingerprint

    Dive into the research topics of 'Light-induced structural changes in a full-length cyanobacterial phytochrome probed by time-resolved X-ray scattering'. Together they form a unique fingerprint.

    Cite this