Evidence map›Paper›PMID 34665262›Full record

ArticleThe Plant cell2022

Thylakoid attachment to the plasma membrane in Synechocystis sp. PCC 6803 requires the AncM protein.

Matthias Ostermeier, Steffen Heinz, Julia Hamm, Jure Zabret, Anna Rast, Andreas Klingl, Marc M Nowaczyk, Jörg Nickelsen

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. On the non-oxygenic origins of thylakoids.Communications biology · 2025
    Review
  5. Article
  6. Review
  7. 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

8 authors at 2 institutions in 1 country.

Matthias OstermeierDepartment of Molecular Plant Science, LMU Munich, Planegg-Martinsried, 82152, Germany.ORCID 0000-0002-9509-1579
Steffen HeinzDepartment of Molecular Plant Science, LMU Munich, Planegg-Martinsried, 82152, Germany.ORCID 0000-0001-9907-3215
Julia HammDepartment of Molecular Plant Science, LMU Munich, Planegg-Martinsried, 82152, Germany.ORCID 0000-0002-9240-6854
Jure ZabretDepartment of Plant Biochemistry, Ruhr-University Bochum, Bochum 44801, Germany.ORCID 0000-0002-4547-4926
Anna RastDepartment of Molecular Plant Science, LMU Munich, Planegg-Martinsried, 82152, Germany.ORCID 0000-0002-3309-1792
Andreas KlinglDepartment of Plant Development, LMU Munich, Planegg-Martinsried, 82152, Germany.ORCID 0000-0001-8414-8317
Marc M NowaczykDepartment of Plant Biochemistry, Ruhr-University Bochum, Bochum 44801, Germany.ORCID 0000-0002-9269-0672
Jörg NickelsenDepartment of Molecular Plant Science, LMU Munich, Planegg-Martinsried, 82152, Germany.ORCID 0000-0003-4184-4560
Urologische Klinik München · DERuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thylakoids are the highly specialized internal membrane systems that harbor the photosynthetic electron transport machinery in cyanobacteria and in chloroplasts. In Synechocystis sp. PCC 6803, thylakoid membranes (TMs) are arranged in peripheral sheets that occasionally converge on the plasma membrane (PM) to form thylakoid convergence membranes (TCMs). TCMs connect several thylakoid sheets and form local contact sites called thylapses between the two membrane systems, at which the early steps of photosystem II (PSII) assembly occur. The protein CurT is one of the main drivers of TCM formation known so far. Here, we identify, by whole-genome sequencing of a curT- suppressor strain, the protein anchor of convergence membranes (AncM) as a factor required for the attachment of thylakoids to the PM at thylapses. An ancM- mutant is shown to have a photosynthetic phenotype characterized by reductions in oxygen-evolution rate, PSII accumulation, and PS assembly. Moreover, the ancM- strain exhibits an altered thylakoid ultrastructure with additional sheets and TCMs detached from the PM. By combining biochemical studies with fluorescence and correlative light-electron microscopy-based approaches, we show that AncM is an integral membrane protein located in biogenic TCMs that form thylapses. These data suggest an antagonistic function of AncM and CurT in shaping TM ultrastructure.

Indexed as

Bacterial ProteinsCell MembraneSynechocystisThylakoidsBacterial Proteins

Identifiers

PMID34665262
PMCPMC8846179
OpenAlexW3206537589

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.