Evidence map›Paper›PMID 25893898›Full record

ArticlePhotosynthesis research2015

D1 fragmentation in photosystem II repair caused by photo-damage of a two-step model.

Yusuke Kato, Shin-Ichiro Ozawa, Yuichiro Takahashi, Wataru Sakamoto

Abstract read
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In one paragraph

Article in Photosynthesis research, 2015. 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
2.1field-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

18 citing papers in PubMed, 49 citations in OpenAlex.

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  5. Enzymes degraded under high light maintain proteostasis by transcriptional regulation inProceedings of the National Academy of Sciences of the United States of America · 2022
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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

4 authors at 1 institution in 1 country.

Yusuke KatoInstitute of Plant Science and Resources (IPSR), Okayama University, 2-20-1 Chuo, Kurashiki, Okayama, 710-0046, Japan.
Shin-Ichiro OzawaGraduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kita-ku, Okayama City, Okayama, 700-8530, Japan.
Yuichiro TakahashiGraduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kita-ku, Okayama City, Okayama, 700-8530, Japan.
Wataru SakamotoInstitute of Plant Science and Resources (IPSR), Okayama University, 2-20-1 Chuo, Kurashiki, Okayama, 710-0046, Japan. saka@rib.okayama-u.ac.jp.
Okayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Light energy drives photosynthesis, but it simultaneously inactivates photosynthetic mechanisms. A major target site of photo-damage is photosystem II (PSII). It further targets one reaction center protein, D1, which is maintained efficiently by the PSII repair cycle. Two proteases, FtsH and Deg, are known to contribute to this process, respectively, by efficient degradation of photo-damaged D1 protein processively and endoproteolytically. This study tested whether the D1 cleavage accomplished by these proteases is affected by different monochromic lights such as blue and red light-emitting-diode light sources, remaining mindful that the use of these lights distinguishes the current models for photoinhibition: the excess-energy model and the two-step model. It is noteworthy that in the two-step model, primary damage results from the absorption of light energy in the Mn-cluster, which can be enhanced by a blue rather than a red light source. Results showed that blue and red lights affect D1 degradation differently. One prominent finding was that D1 fragmentation that is specifically generated by luminal Deg proteases was enhanced by blue light but not by red light in the mutant lacking FtsH2. Although circumstantial, this evidence supports a two-step model of PSII photo-damage. We infer that enhanced D1 fragmentation by luminal Deg proteases is a response to primary damage at the Mn-cluster.

Indexed as

ArabidopsisChloroplast ProteinsChloroplastsLightModels, BiologicalPeptide HydrolasesPhotosynthesisPhotosystem II Protein ComplexChloroplast ProteinsPeptide HydrolasesPhotosystem II Protein ComplexChloroplast proteaseD1 degradationDegFtsHPhotoinhibitionPSII repair

Identifiers

PMID25893898
OpenAlexW1972564399

What OpenQuestion holds

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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.