Evidence map›Paper›PMID 34910272›Full record

ArticlePhotosynthesis research2022

Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification.

Jan Lambertz, Pasqual Liauw, Julian P Whitelegge, Marc M Nowaczyk

Abstract read
In one paragraph

Article in Photosynthesis research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
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  3. Review
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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.

Jan Lambertz *Plant Biochemistry, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Bochum, Germany.ORCID http://orcid.org/0000-0002-2722-2370
Pasqual Liauw *Plant Biochemistry, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Bochum, Germany.
Julian P WhiteleggeThe Pasarow Mass Spectrometry Laboratory, David Geffen School of Medicine, The Jane and Terry Semel Institute for Neuroscience and Human Behavior, UCLA, Los Angeles, CA, 90095, USA.ORCID http://orcid.org/0000-0003-2763-7733
Marc M NowaczykPlant Biochemistry, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Bochum, Germany. marc.m.nowaczyk@rub.de.ORCID http://orcid.org/0000-0002-9269-0672

Funding

Deutsche Forschungsgemeinschaft NO 836/3-1
6 · The paper itself

Abstract

The assembly of large, multi-cofactor membrane protein complexes like photosystem II (PSII) requires a high level of coordination. The process is facilitated by a large network of auxiliary proteins that bind transiently to unassembled subunits, preassembled modules or intermediate states of PSII, which are comprised of a subset of subunits. However, analysis of these immature, partially assembled PSII complexes is hampered by their low abundance and intrinsic instability. In this study, PSII was purified from the thermophilic cyanobacterium Thermosynechococcus elongatus via Twin-Strep-tagged CP43 and further separated by ion exchange chromatography into mature and immature complexes. Mass spectrometry analysis of the immature Psb27-PSII intermediate revealed six different Psb27 proteoforms with distinct lipid modifications. The maturation and functional role of thylakoid localized lipoproteins are discussed.

Indexed as

CyanobacteriaPhotosystem II Protein ComplexBacterial ProteinsLipidsMass SpectrometryPhotosynthesisBacterial ProteinsLipidsPhotosystem II Protein ComplexCyanobacteriaLipoproteinMass spectrometryPhotosynthesisPsb27

Identifiers

PMID34910272
PMCPMC9458691

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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.