Evidence map›Paper›PMID 36065640›Full record

ArticleeLife2022

Proton-transporting heliorhodopsins from marine giant viruses.

Shoko Hososhima, Ritsu Mizutori, Rei Abe-Yoshizumi, Andrey Rozenberg, Shunta Shigemura, Alina Pushkarev, Masae Konno, Kota Katayama, Keiichi Inoue, Satoshi P Tsunoda and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Molecular properties of a viral heliorhodopsin, V2HeR2.Biophysics and physicobiology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

12 authors at 2 institutions in 2 countries.

Shoko HososhimaDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0001-7465-2907
Ritsu MizutoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.
Rei Abe-YoshizumiDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0002-7082-7949
Andrey RozenbergFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Shunta ShigemuraDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.
Alina PushkarevFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Masae KonnoDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.
Kota KatayamaDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.
Keiichi InoueDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0002-6898-4347
Satoshi P TsunodaDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0003-3636-1521
Oded BéjàFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0001-6629-0192
Hideki KandoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0002-4922-1344
Nagoya Institute of Technology · JPTechnion – Israel Institute of Technology · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rhodopsins convert light into signals and energy in animals and microbes. Heliorhodopsins (HeRs), a recently discovered new rhodopsin family, are widely present in archaea, bacteria, unicellular eukaryotes, and giant viruses, but their function remains unknown. Here, we report that a viral HeR from Emiliania huxleyi virus 202 (V2HeR3) is a light-activated proton transporter. V2HeR3 absorbs blue-green light, and the active intermediate contains the deprotonated retinal Schiff base. Site-directed mutagenesis study revealed that E191 in TM6 constitutes the gate together with the retinal Schiff base. E205 and E215 form a PAG of the Schiff base, and mutations at these positions converted the protein into an outward proton pump. Three environmental viral HeRs from the same group as well as a more distantly related HeR exhibited similar proton-transport activity, indicating that HeR functions might be diverse similarly to type-1 microbial rhodopsins. Some strains of

Indexed as

Giant VirusesProtonsAnimalsIon TransportRhodopsinRhodopsins, MicrobialSchiff BasesheliorhodopsinProtonsRhodopsinRhodopsins, MicrobialSchiff BasesE. huxleyi virusmolecular biophysicsneuroscienceoptogeneticspatch clampproton channelrhodopsinstructural biologystructural change

Identifiers

PMID36065640
PMCPMC9448325
OpenAlexW4293037587

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.