Evidence map›Paper›PMID 37986577›Full record

ArticleeLife2023

Characterization of tryptophan oxidation affecting D1 degradation by FtsH in the photosystem II quality control of chloroplasts.

Yusuke Kato, Hiroshi Kuroda, Shin-Ichiro Ozawa, Keisuke Saito, Vivek Dogra, Martin Scholz, Guoxian Zhang, Catherine de Vitry, Hiroshi Ishikita, Chanhong Kim and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 13 citations in OpenAlex.

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  15. Genes · 2024
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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

13 authors at 6 institutions in 8 countries.

Yusuke Kato *Institute of Plant Science and Resources (IPSR), Okayama University, Okayama, Japan.ORCID 0000-0003-1718-9121
Hiroshi Kuroda *Research Institute for Interdisciplinary Science, Okayama University, Okayama, Japan.
Shin-Ichiro Ozawa *Institute of Plant Science and Resources (IPSR), Okayama University, Okayama, Japan.ORCID 0000-0001-7698-5350
Keisuke SaitoResearch Center for Advanced Science and Technology, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-2293-9743
Vivek DograShanghai Center for Plant Stress Biology, Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0003-1853-8274
Martin ScholzInstitute of Plant Biology and Biotechnology, University of Münster, Münster, Germany.
Guoxian ZhangInstitute of Plant Science and Resources (IPSR), Okayama University, Okayama, Japan.
Catherine de VitryInstitut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, Centre National de la Recherche Scientifique and Sorbonne Université Pierre et Marie Curie, Paris, France.
Hiroshi IshikitaResearch Center for Advanced Science and Technology, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-5849-8150
Chanhong KimShanghai Center for Plant Stress Biology, Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0003-4133-9070
Michael HipplerInstitute of Plant Science and Resources (IPSR), Okayama University, Okayama, Japan.ORCID 0000-0001-9670-6101
Yuichiro TakahashiResearch Institute for Interdisciplinary Science, Okayama University, Okayama, Japan.
Wataru SakamotoInstitute of Plant Science and Resources (IPSR), Okayama University, Okayama, Japan.ORCID 0000-0001-9747-5042
Okayama University · JPChinese Academy of Sciences · CNThe University of Tokyo · JPSetsunan University · JPSorbonne Université · FRUniversity of Münster · DE

Funding

Agence Nationale de la Recherche ANR-11-LABX-0011-01Japan Society for the Promotion of Science KAKENHI (20H03217)Japan Society for the Promotion of Science KAKENHI (21H02508)Japan Society for the Promotion of Science KAKENHI (21K06221)Japan Society for the Promotion of Science KAKENHI (23H02444)Ministry of Education, Culture, Sports, Science and Technology KAKENHI (23H04959)Ministry of Education, Culture, Sports, Science and Technology KAKENHI (23H04963)Sorbonne Université UMR7141
6 · The paper itself

Abstract

Photosynthesis is one of the most important reactions for sustaining our environment. Photosystem II (PSII) is the initial site of photosynthetic electron transfer by water oxidation. Light in excess, however, causes the simultaneous production of reactive oxygen species (ROS), leading to photo-oxidative damage in PSII. To maintain photosynthetic activity, the PSII reaction center protein D1, which is the primary target of unavoidable photo-oxidative damage, is efficiently degraded by FtsH protease. In PSII subunits, photo-oxidative modifications of several amino acids such as Trp have been indeed documented, whereas the linkage between such modifications and D1 degradation remains elusive. Here, we show that an oxidative post-translational modification of Trp residue at the N-terminal tail of D1 is correlated with D1 degradation by FtsH during high-light stress. We revealed that

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsLightMetalloendopeptidasesPhotosystem II Protein ComplexTryptophanArabidopsis ProteinsFtsH protein, ArabidopsisMetalloendopeptidasesPhotosystem II Protein ComplexTryptophanArabidopsis thalianachlamydomonas reinhardtiiphoto-oxidative damagephotosystem IIplant biologypost-translational modificationprotein degradationtryptophan oxidation

Identifiers

PMID37986577
PMCPMC10665015
OpenAlexW4385289643

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.