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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-01-03

AUTHORS

Derren J. Heyes, Samantha J. O. Hardman, Martin N. Pedersen, Joyce Woodhouse, Eugenio De La Mora, Michael Wulff, Martin Weik, Marco Cammarata, Nigel S. Scrutton, Giorgio Schirò

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. More... »

PAGES

1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-018-0242-0

DOI

http://dx.doi.org/10.1038/s42003-018-0242-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1110929205

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30740537


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