Evidence map›Paper›PMID 26508763›Full record

ArticleThe Plant cell2015

Light-Harvesting Complex Stress-Related Proteins Catalyze Excess Energy Dissipation in Both Photosystems of Physcomitrella patens.

Alberta Pinnola, Stefano Cazzaniga, Alessandro Alboresi, Reinat Nevo, Smadar Levin-Zaidman, Ziv Reich, Roberto Bassi

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 67 citations in OpenAlex.

  1. LHCSR1 Functions as a Dimmer Switch for Light Harvesting.The journal of physical chemistry letters · 2026
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  14. Photoprotection mechanisms under different COPhotosynthesis research · 2020
    Article
  15. Article
  16. A Chloroplast COR413 Protein FromFrontiers in plant science · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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

7 authors at 2 institutions in 2 countries.

Alberta PinnolaDepartment of Biotechnology, University of Verona, 37134 Verona, Italy.ORCID http://orcid.org/0000-0001-8373-7638
Stefano CazzanigaDepartment of Biotechnology, University of Verona, 37134 Verona, Italy.
Alessandro AlboresiDepartment of Biotechnology, University of Verona, 37134 Verona, Italy.ORCID http://orcid.org/0000-0003-4818-7778
Reinat NevoDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Smadar Levin-ZaidmanElectron Microscopy Unit, Weizmann Institute of Science, Rehovot 76100, Israel.
Ziv ReichDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Roberto BassiDepartment of Biotechnology, University of Verona, 37134 Verona, Italy roberto.bassi@univr.it.ORCID http://orcid.org/0000-0002-4140-8446
University of Verona · ITWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two LHC-like proteins, Photosystem II Subunit S (PSBS) and Light-Harvesting Complex Stress-Related (LHCSR), are essential for triggering excess energy dissipation in chloroplasts of vascular plants and green algae, respectively. The mechanism of quenching was studied in Physcomitrella patens, an early divergent streptophyta (including green algae and land plants) in which both proteins are active. PSBS was localized in grana together with photosystem II (PSII), but LHCSR was located mainly in stroma-exposed membranes together with photosystem I (PSI), and its distribution did not change upon high-light treatment. The quenched conformation can be preserved by rapidly freezing the high-light-treated tissues in liquid nitrogen. When using green fluorescent protein as an internal standard, 77K fluorescence emission spectra on isolated chloroplasts allowed for independent assessment of PSI and PSII fluorescence yield. Results showed that both photosystems underwent quenching upon high-light treatment in the wild type in contrast to mutants depleted of LHCSR, which lacked PSI quenching. Due to the contribution of LHCII, P. patens had a PSI antenna size twice as large with respect to higher plants. Thus, LHCII, which is highly abundant in stroma membranes, appears to be the target of quenching by LHCSR.

Indexed as

Stress, PhysiologicalBryopsidaCatalysisChlorophyllChloroplastsDigitoninGlucosidesLightLight-Harvesting Protein ComplexesMembrane MicrodomainsPhotochemical ProcessesPhotosystem II Protein ComplexPhotosystem I Protein ComplexPlant ProteinsSpectrometry, FluorescenceThermodynamicsChlorophyllDigitonindodecyl maltosideGlucosidesLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexPhotosystem I Protein ComplexPlant Proteins

Identifiers

PMID26508763
PMCPMC4682295
OpenAlexW1851286588

What OpenQuestion holds

Textmetadata
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.