Evidence map›Paper›PMID 39801362›Full record

ArticleThe FEBS journal2025

Dual-Cys bacteriophytochromes: intermediates in cyanobacterial phytochrome evolution?

Hee Wook Yang, Ji-Young Song, Ji-Joon Song, Young Won Kim, Nathan C Rockwell, Woojin Kim, Hyunsoo Kim, J Clark Lagarias, Youn-Il Park

Abstract read
In one paragraph

Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Circular dichroism spectroscopy reveals multiple phytochrome photoproducts in equilibrium.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    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

9 authors.

Hee Wook YangDepartment of Biological Sciences, Chungnam National University, Daejeon, Korea.
Ji-Young SongDepartment of Biological Sciences, Chungnam National University, Daejeon, Korea.
Ji-Joon SongDepartment of Biological Science and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.ORCID 0000-0001-7120-6311
Young Won KimDepartment of Biological Sciences, Chungnam National University, Daejeon, Korea.
Nathan C RockwellDepartment of Molecular and Cellular Biology, University of California, Davis, CA, USA.
Woojin KimDepartment of Convergent Bioscience and Informatics, Chungnam National University, Daejeon, Korea.
Hyunsoo KimDepartment of Convergent Bioscience and Informatics, Chungnam National University, Daejeon, Korea.
J Clark LagariasDepartment of Molecular and Cellular Biology, University of California, Davis, CA, USA.ORCID 0000-0002-2093-0403
Youn-Il ParkDepartment of Biological Sciences, Chungnam National University, Daejeon, Korea.ORCID 0000-0003-2912-2821

Funding

UNDERSTANDING AND LEVERAGING MOLECULAR DIVERSITY WITHIN THE PHYTOCHROME SUPERFAMILYR35GM139598 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LAGARIAS, JOHN CLARK · 2021 to 2025
$2.0M
Chungnam National UniversityKRIBB Research Initiative Program KGM1002311NIGMS-NIH R35GM139598NIGMS NIH HHS R35 GM139598
6 · The paper itself

Abstract

Previous studies have identified three families of knotted phytochrome photoreceptors in cyanobacteria. We describe a fourth type: 'hybrid' phytochromes with putative bilin-binding cysteine residues in both their N-terminal 'knot' extensions and cGMP-phosphodiesterase/adenylate cyclase/FhlA (GAF) domains, which we designate as dual-cysteine bacteriophytochromes (DCBs). Recombinant expression of DCBs in Escherichia coli yields photoactive phycocyanobilin (PCB) adducts with red/far-red photocycles similar to those of the GAF-Cys-containing cyanobacterial phytochromes (Cph1s). Incorporation of the PCB precursor, biliverdin IXα (BV), gave multiple populations, one of which appears similar to those of cyanobacterial bacteriophytochromes (cBphPs). A crystal structure of FiDCB bound to BV exhibits two thioether linkages between the GAF- and 'PAS-knot'-Cys residues and the C3

Indexed as

Bacterial ProteinsCyanobacteriaCysteineEvolution, MolecularPhytochromeAmino Acid SequenceBiliverdineCrystallography, X-RayEscherichia coliModels, MolecularPhycobilinsPhycocyaninRecombinant ProteinsBacterial ProteinsBiliverdineCysteinePhycobilinsPhycocyaninphycocyanobilinPhytochromeRecombinant Proteinscrystal structurecyanobacterial phytochromesdual‐cysteine bacteriophytochromessite‐directed mutagenesis

Identifiers

PMID39801362
PMCPMC11880981

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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.