Evidence map›Paper›PMID 30948637›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Rational conversion of chromophore selectivity of cyanobacteriochromes to accept mammalian intrinsic biliverdin.

Keiji Fushimi, Takatsugu Miyazaki, Yuto Kuwasaki, Takahiro Nakajima, Tatsuro Yamamoto, Kazushi Suzuki, Yoshibumi Ueda, Keita Miyake, Yuka Takeda, Jae-Hoon Choi and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Discovery and Engineering of Unique Cyanobacteriochrome GAF Domains.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Article
  6. Cyanobacteriochromes: A Rainbow of Photoreceptors.Annual review of microbiology · 2024
    Review
  7. Article
  8. Red/green cyanobacteriochromes acquire isomerization from phycocyanobilin to phycoviolobilin.Protein science : a publication of the Protein Society · 2024
    Article
  9. Photocobilins integrate BNature communications · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Novel cyanobacteriochrome photoreceptor with the second Cys residue showing atypical orange/blue reversible photoconversion.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  16. Light- and pH-dependent structural changes in cyanobacteriochrome AnPixJg2.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  17. Protein-chromophore interactions controlling photoisomerization in red/green cyanobacteriochromes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  18. Article
  19. Article
  20. Review
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

15 authors at 2 institutions in 1 country.

Keiji FushimiGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Takatsugu MiyazakiGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Yuto KuwasakiGraduate School of Arts and Sciences, University of Tokyo, 153-8902 Tokyo, Japan.
Takahiro NakajimaGraduate School of Arts and Sciences, University of Tokyo, 153-8902 Tokyo, Japan.
Tatsuro YamamotoGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Kazushi SuzukiGraduate School of Arts and Sciences, University of Tokyo, 153-8902 Tokyo, Japan.
Yoshibumi UedaGraduate School of Arts and Sciences, University of Tokyo, 153-8902 Tokyo, Japan.
Keita MiyakeGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Yuka TakedaGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Jae-Hoon ChoiGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Hirokazu KawagishiGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Enoch Y ParkGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan.
Masahiko IkeuchiCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kawaguchi, 332-0012 Saitama, Japan.
Moritoshi SatoCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kawaguchi, 332-0012 Saitama, Japan.
Rei NarikawaGraduate School of Integrated Science and Technology, Shizuoka University, 422-8529 Shizuoka, Japan; narikawa.rei@shizuoka.ac.jp.ORCID 0000-0001-7891-3510
Shizuoka University · JPTokyo University of the Arts · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Because cyanobacteriochrome photoreceptors need only a single compact domain for chromophore incorporation and for absorption of visible spectra including the long-wavelength far-red region, these molecules have been paid much attention for application to bioimaging and optogenetics. Most cyanobacteriochromes, however, have a drawback to incorporate phycocyanobilin that is not available in the mammalian cells. In this study, we focused on biliverdin (BV) that is a mammalian intrinsic chromophore and absorbs the far-red region and revealed that replacement of only four residues was enough for conversion from BV-rejective cyanobacteriochromes into BV-acceptable molecules. We succeeded in determining the crystal structure of one of such engineered molecules, AnPixJg2_BV4, at 1.6 Å resolution. This structure identified unusual covalent bond linkage, which resulted in deep BV insertion into the protein pocket. The four mutated residues contributed to reducing steric hindrances derived from the deeper insertion. We introduced these residues into other domains, and one of them, NpF2164g5_BV4, produced bright near-infrared fluorescence from mammalian liver in vivo. Collectively, this study provides not only molecular basis to incorporate BV by the cyanobacteriochromes but also rational strategy to open the door for application of cyanobacteriochromes to visualization and regulation of deep mammalian tissues.

Indexed as

BiliverdinePhotoreceptors, MicrobialAnimalsChlorocebus aethiopsCOS CellsCyanobacteriaGreen Fluorescent ProteinsLiverMiceModels, MolecularOptical ImagingProtein EngineeringRecombinant ProteinsTransfectionBiliverdineGreen Fluorescent ProteinsPhotoreceptors, MicrobialRecombinant Proteinsbilinin vivo imagingprotein engineering

Identifiers

PMID30948637
PMCPMC6486744
OpenAlexW2931041725

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.