Evidence map›Paper›PMID 33554065›Full record

ArticleiScience2021

The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I.

Mai Duy Luu Trinh, Daichi Miyazaki, Sumire Ono, Jiro Nomata, Masaru Kono, Hiroyuki Mino, Tatsuya Niwa, Yuki Okegawa, Ken Motohashi, Hideki Taguchi and 2 more

Open access · goldAbstract read
In one paragraph

Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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

12 authors at 4 institutions in 1 country.

Mai Duy Luu TrinhDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Daichi MiyazakiDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Sumire OnoDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Jiro NomataLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Masaru KonoDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Hiroyuki MinoDivision of Materials Science (Physics), Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Tatsuya NiwaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Yuki OkegawaDepartment of Frontier Life Sciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.
Ken MotohashiDepartment of Frontier Life Sciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.
Hideki TaguchiCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Toru HisaboriLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Shinji MasudaDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Tokyo Institute of Technology · JPKyoto Sangyo University · JPNagoya University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In natural habitats, plants have developed sophisticated regulatory mechanisms to optimize the photosynthetic electron transfer rate at the maximum efficiency and cope with the changing environments. Maintaining proper P700 oxidation at photosystem I (PSI) is the common denominator for most regulatory processes of photosynthetic electron transfers. However, the molecular complexes and cofactors involved in these processes and their function(s) have not been fully clarified. Here, we identified a redox-active chloroplast protein, the triplet-cysteine repeat protein (TCR). TCR shared similar expression profiles with known photosynthetic regulators and contained two triplet-cysteine motifs (CxxxCxxxC). Biochemical analysis indicated that TCR localizes in chloroplasts and has a [3Fe-4S] cluster. Loss of TCR limited the electron sink downstream of PSI during dark-to-light transition.

Indexed as

Biological sciencesplant biologyplant geneticsplant physiology

Identifiers

PMID33554065
PMCPMC7848650
OpenAlexW3119394791

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.