Evidence map›Paper›PMID 25971964›Full record

ArticleThe Journal of biological chemistry2015

Light-induced Changes in the Dimerization Interface of Bacteriophytochromes.

Heikki Takala, Alexander Björling, Marko Linna, Sebastian Westenhoff, Janne A Ihalainen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
11.9field-weighted citation impact, top 2% of its field
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

25 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  6. The structural effect between the output module and chromophore-binding domain is a two-way street via the hairpin extension.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Phytochrome Signaling Networks.Annual review of plant biology · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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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

5 authors at 2 institutions in 2 countries.

Heikki TakalaFrom the University of Gothenburg, Department of Chemistry and Molecular Biology, Gothenburg, SE-40530 Sweden and University of Jyvaskyla, Nanoscience Center, Department of Biological and Environmental Sciences, Jyväskylä, FI-40014 Finland.
Alexander BjörlingFrom the University of Gothenburg, Department of Chemistry and Molecular Biology, Gothenburg, SE-40530 Sweden and.
Marko LinnaUniversity of Jyvaskyla, Nanoscience Center, Department of Biological and Environmental Sciences, Jyväskylä, FI-40014 Finland.
Sebastian WestenhoffFrom the University of Gothenburg, Department of Chemistry and Molecular Biology, Gothenburg, SE-40530 Sweden and westenho@chem.gu.se.
Janne A IhalainenUniversity of Jyvaskyla, Nanoscience Center, Department of Biological and Environmental Sciences, Jyväskylä, FI-40014 Finland janne.ihalainen@jyu.fi.
University of Jyväskylä · FIUniversity of Gothenburg · SE

Funding

European Research Council 279944
6 · The paper itself

Abstract

Phytochromes are dimeric photoreceptor proteins that sense red light levels in plants, fungi, and bacteria. The proteins are structurally divided into a light-sensing photosensory module consisting of PAS, GAF, and PHY domains and a signaling output module, which in bacteriophytochromes typically is a histidine kinase (HK) domain. Existing structural data suggest that two dimerization interfaces exist between the GAF and HK domains, but their functional roles remain unclear. Using mutational, biochemical, and computational analyses of the Deinococcus radiodurans phytochrome, we demonstrate that two dimerization interfaces between sister GAF and HK domains stabilize the dimer with approximately equal contributions. The existence of both dimerization interfaces is critical for thermal reversion back to the resting state. We also find that a mutant in which the interactions between the GAF domains were removed monomerizes under red light. This implies that the interactions between the HK domains are significantly altered by photoconversion. The results suggest functional importance of the dimerization interfaces in bacteriophytochromes.

Indexed as

Bacterial ProteinsCrystallography, X-RayDeinococcusDimerizationHistidine KinaseLightPhytochromeProtein ConformationProtein KinasesProtein Structure, TertiaryBacterial ProteinsHistidine KinasePhytochromeProtein Kinasescell signalingdimerizationhigh performance liquid chromatography (HPLC)histidine kinasemolecular dynamicsmutagenesisphotoreceptorphytochromeprotein conformationx-ray scattering

Identifiers

PMID25971964
PMCPMC4481235
OpenAlexW1604278147

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.