Evidence map›Paper›PMID 39305959›Full record

ArticleThe Journal of biological chemistry2024

Light-driven anion-pumping rhodopsin with unique cytoplasmic anion-release mechanism.

Tomohiro Ishizuka, Kano Suzuki, Masae Konno, Keisei Shibata, Yuma Kawasaki, Hidefumi Akiyama, Takeshi Murata, Keiichi Inoue

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Tomohiro IshizukaThe Institute for Solid State Physics, The University of Tokyo, Chiba, Japan.
Kano SuzukiDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.
Masae KonnoThe Institute for Solid State Physics, The University of Tokyo, Chiba, Japan; PRESTO, Japan Science and Technology Agency, Saitama, Japan.
Keisei ShibataThe Institute for Solid State Physics, The University of Tokyo, Chiba, Japan.
Yuma KawasakiThe Institute for Solid State Physics, The University of Tokyo, Chiba, Japan.
Hidefumi AkiyamaThe Institute for Solid State Physics, The University of Tokyo, Chiba, Japan.
Takeshi MurataDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan; Membrane Protein Research and Molecular Chirality Research Centers, Chiba University, Chiba, Japan. Electronic address: t.murata@faculty.chiba-u.jp.
Keiichi InoueThe Institute for Solid State Physics, The University of Tokyo, Chiba, Japan. Electronic address: inoue@issp.u-tokyo.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial rhodopsins are photoreceptive membrane proteins found in microorganisms with an all-trans-retinal chromophore. The function of many microbial rhodopsins is determined by three residues in the third transmembrane helix called motif residues. Here, we report a group of microbial rhodopsins with a novel Thr-Thr-Gly (TTG) motif. The ion-transport assay revealed that they function as light-driven inward anion pumps similar to halorhodopsins previously found in archaea and bacteria. Based on the characteristic glycine residue in their motif and light-driven anion-pumping function, these new rhodopsins are called glycylhalorhodopsins (GHRs). X-ray crystallographic analysis found large cavities on the cytoplasmic side, which are produced by the small side-chain volume of the glycine residue in the motif. The opened structure of GHR on the cytoplasmic side is related to the anion releasing process to the cytoplasm during the photoreaction compared to canonical halorhodopsin from Natronomonas pharaonis (NpHR). GHR also transports SO

Indexed as

AnionsLightAmino Acid MotifsArchaeal ProteinsCrystallography, X-RayCytoplasmHalobacteriaceaeIon TransportRhodopsins, MicrobialAnionsArchaeal ProteinsRhodopsins, Microbialanion pumpmicrobial rhodopsinphotoreceptorrhodopsinspectroscopyX-ray crystallography

Identifiers

PMID39305959
PMCPMC11532467

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Registered trials

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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.