Evidence map›Paper›PMID 30740537›Full record

ArticleCommunications biology2019

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

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 read
In one paragraph

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
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  11. Using photocaging for fast time-resolved structural biology studies.Acta crystallographica. Section D, Structural biology · 2021
    Review
  12. Time-resolved X-ray scattering studies of proteins.Current opinion in structural biology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Photoreversible interconversion of a phytochrome photosensory module in the crystalline state.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Derren J Heyes1Manchester Institute of Biotechnology, University of Manchester, 131 Princess St, Manchester, M1 7DN UK.ORCID 0000-0002-7453-1571
Samantha J O Hardman1Manchester Institute of Biotechnology, University of Manchester, 131 Princess St, Manchester, M1 7DN UK.
Martin N Pedersen2European Synchrotron Radiation Facility, 71 Avenue des Martyrs, 38044 Grenoble, France.
Joyce Woodhouse3Institut de Biologie Structurale, CNRS, Univ. Grenoble Alpes, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.
Eugenio De La Mora3Institut de Biologie Structurale, CNRS, Univ. Grenoble Alpes, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.
Michael Wulff2European Synchrotron Radiation Facility, 71 Avenue des Martyrs, 38044 Grenoble, France.
Martin Weik3Institut de Biologie Structurale, CNRS, Univ. Grenoble Alpes, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.ORCID 0000-0001-9297-642X
Marco Cammarata4Univ. Rennes 1, CNRS, UBL, Institut de Physique de Rennes (IPR) - UMR 6251, 263 avenue du Général Leclerc, 35042 Rennes, France.ORCID 0000-0003-3013-1186
Nigel S Scrutton1Manchester Institute of Biotechnology, University of Manchester, 131 Princess St, Manchester, M1 7DN UK.
Giorgio Schirò3Institut de Biologie Structurale, CNRS, Univ. Grenoble Alpes, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

LightScattering, RadiationBacterial ProteinsDeinococcusKineticsModels, MolecularPhotoreceptors, MicrobialPhytochromeProtein ConformationProtein KinasesSignal TransductionSynechocystisX-Ray Absorption SpectroscopyX-RaysBacterial ProteinsCph1 phytochrome protein, bacteriaPhotoreceptors, MicrobialPhytochromeProtein Kinases

Identifiers

PMID30740537
PMCPMC6318211

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.