Evidence map›Paper›PMID 20923938›Full record

ArticleThe Plant cell2010

The Arabidopsis thylakoid protein PAM68 is required for efficient D1 biogenesis and photosystem II assembly.

Ute Armbruster, Jessica Zühlke, Birgit Rengstl, Renate Kreller, Elina Makarenko, Thilo Rühle, Danja Schünemann, Peter Jahns, Bernd Weisshaar, Jörg Nickelsen and 1 more

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

82 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Review
  3. The lumenal domain of Cyt bPhotosynthesis research · 2025
    Article
  4. Article
  5. Article
  6. Defining the heterogeneous composition of Arabidopsis thylakoid membrane.The Plant journal : for cell and molecular biology · 2025
    Article
  7. Review
  8. The variegatedComputational and structural biotechnology journal · 2024
    Article
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  11. Article
  12. Review
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  14. Review
  15. Article
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22 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 1 country.

Ute ArmbrusterLehrstuhl für Molekularbiologie der Pflanzen (Botanik), Department Biologie I, Ludwig-Maximilians-Universität, Martinsried, Germany.
Jessica Zühlke
Birgit Rengstl
Renate Kreller
Elina Makarenko
Thilo Rühle
Danja Schünemann
Peter Jahns
Bernd Weisshaar
Jörg Nickelsen
Dario Leister
Ludwig-Maximilians-Universität München · DEBielefeld University · DEHeinrich Heine University Düsseldorf · DERuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem II (PSII) is a multiprotein complex that functions as a light-driven water:plastoquinone oxidoreductase in photosynthesis. Assembly of PSII proceeds through a number of distinct intermediate states and requires auxiliary proteins. The photosynthesis affected mutant 68 (pam68) of Arabidopsis thaliana displays drastically altered chlorophyll fluorescence and abnormally low levels of the PSII core subunits D1, D2, CP43, and CP47. We show that these phenotypes result from a specific decrease in the stability and maturation of D1. This is associated with a marked increase in the synthesis of RC (the PSII reaction center-like assembly complex) at the expense of PSII dimers and supercomplexes. PAM68 is a conserved integral membrane protein found in cyanobacterial and eukaryotic thylakoids and interacts in split-ubiquitin assays with several PSII core proteins and known PSII assembly factors. Biochemical analyses of thylakoids from Arabidopsis and Synechocystis sp PCC 6803 suggest that, during PSII assembly, PAM68 proteins associate with an early intermediate complex that might contain D1 and the assembly factor LPA1. Inactivation of cyanobacterial PAM68 destabilizes RC but does not affect larger PSII assembly complexes. Our data imply that PAM68 proteins promote early steps in PSII biogenesis in cyanobacteria and plants, but their inactivation is differently compensated for in the two classes of organisms.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsDNA, PlantGene Expression Regulation, PlantMolecular Sequence DataMutagenesis, InsertionalMutationPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSequence AlignmentSynechocystisThylakoidsArabidopsis ProteinsDNA, PlantPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein Complex

Identifiers

PMID20923938
PMCPMC2990134
OpenAlexW2122908352

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.