Evidence map›Paper›PMID 36190943›Full record

ArticlePLoS biology2022

Heliorhodopsin binds and regulates glutamine synthetase activity.

Shin-Gyu Cho, Myungchul Song, Kimleng Chuon, Jin-Gon Shim, Seanghun Meas, Kwang-Hwan Jung

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular properties of a viral heliorhodopsin, V2HeR2.Biophysics and physicobiology · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. 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

6 authors at 1 institution in 2 countries.

Shin-Gyu ChoDepartment of Life Science and Institute of Biological Interfaces, Sogang University, Seoul, Korea.
Myungchul SongDepartment of Life Science and Institute of Biological Interfaces, Sogang University, Seoul, Korea.
Kimleng ChuonDepartment of Life Science and Institute of Biological Interfaces, Sogang University, Seoul, Korea.
Jin-Gon ShimDepartment of Life Science and Institute of Biological Interfaces, Sogang University, Seoul, Korea.
Seanghun MeasDepartment of Life Science and Institute of Biological Interfaces, Sogang University, Seoul, Korea.
Kwang-Hwan JungDepartment of Life Science and Institute of Biological Interfaces, Sogang University, Seoul, Korea.ORCID 0000-0002-0828-6539
Sogang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photoreceptors are light-sensitive proteins found in various organisms that respond to light and relay signals into the cells. Heliorhodopsin, a retinal-binding membrane protein, has been recently discovered, however its function remains unknown. Herein, we investigated the relationship between Actinobacteria bacterium IMCC26103 heliorhodopsin (AbHeR) and an adjacent glutamine synthetase (AbGS) in the same operon. We demonstrate that AbHeR binds to AbGS and regulates AbGS activity. More specifically, the dissociation constant (Kd) value of the binding between AbHeR and AbGS is 6.06 μM. Moreover, the absence of positively charged residues within the intracellular loop of AbHeR impacted Kd value as they serve as critical binding sites for AbGS. We also confirm that AbHeR up-regulates the biosynthetic enzyme activity of AbGS both in vitro and in vivo in the presence of light. GS is a key enzyme involved in nitrogen assimilation that catalyzes the conversion of glutamate and ammonia to glutamine. Hence, the interaction between AbHeR and AbGS may be critical for nitrogen assimilation in Actinobacteria bacterium IMCC26103 as it survives in low-nutrient environments. Overall, the findings of our study describe, for the first time, to the best of our knowledge, a novel function of heliorhodopsin as a regulatory rhodopsin with the capacity to bind and regulate enzyme activity required for nitrogen assimilation.

Indexed as

Glutamate-Ammonia LigaseGlutamineAmmoniaGlutamic AcidNitrogenRhodopsinRhodopsins, MicrobialAmmoniaGlutamate-Ammonia LigaseGlutamic AcidGlutamineheliorhodopsinNitrogenRhodopsinRhodopsins, Microbial

Identifiers

PMID36190943
PMCPMC9529153
OpenAlexW4300688669

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.