Evidence map›Paper›PMID 29123155›Full record

ArticleScientific reports2017

Large-scale in vitro production, refolding and dimerization of PsbS in different microenvironments.

Maithili Krishnan, Geri F Moolenaar, Karthick Babu Sai Sankar Gupta, Nora Goosen, Anjali Pandit

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. pH-Dependent Conformational Switch Impacts Stability of the PsbS Dimer.The journal of physical chemistry letters · 2023
    Article
  4. Article
  5. 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

5 authors.

Maithili KrishnanLeiden University, Leiden Institute of Chemistry, Gorlaeus Laboratories, Einsteinweg, 55 2333 CC, Leiden, The Netherlands.
Geri F MoolenaarLeiden University, Leiden Institute of Chemistry, Gorlaeus Laboratories, Einsteinweg, 55 2333 CC, Leiden, The Netherlands.
Karthick Babu Sai Sankar GuptaLeiden University, Leiden Institute of Chemistry, Gorlaeus Laboratories, Einsteinweg, 55 2333 CC, Leiden, The Netherlands.
Nora GoosenLeiden University, Leiden Institute of Chemistry, Gorlaeus Laboratories, Einsteinweg, 55 2333 CC, Leiden, The Netherlands.
Anjali PanditLeiden University, Leiden Institute of Chemistry, Gorlaeus Laboratories, Einsteinweg, 55 2333 CC, Leiden, The Netherlands. a.pandit@lic.leidenuniv.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants adapt to fluctuating light conditions by a process called non-photochemical quenching (NPQ), where membrane protein PsbS plays a crucial role and transforms a change in the pH-gradient across the thylakoid membrane under excess light conditions into a photoprotective state, leading to de-excitation of antenna chlorophylls. The PsbS activation mechanism is elusive and has been proposed to involve a monomerization step and protonation of specific residues. To elucidate its function, it is essential to produce PsbS in large quantities, stabilize PsbS in a membrane-mimicking environment and analyze its pH-dependent conformational structure. We present an approach for large-scale in-vitro production and spectroscopic characterization of PsbS under controlled, non-crystalline conditions. We produced PsbS of the moss Physcomitrella patens in milligram quantities in E. coli, refolded PsbS in several detergent types and analyzed its conformation at neutral and low pH by Dynamic Light Scattering and NMR spectroscopy. Our results reveal that at both pH conditions, PsbS exist as dimers or in apparent monomer-dimer equilibria. Lowering of the pH induces conformational changes, destabilizes the dimer state and shifts the equilibria towards the monomeric form. In vivo, a similar response upon thylakoid lumen acidification may tune PsbS activity in a gradual manner.

Indexed as

BryopsidaProtein FoldingProtein MultimerizationDynamic Light ScatteringEscherichia coliHydrogen-Ion ConcentrationMagnetic Resonance SpectroscopyPlant ProteinsProtein ConformationRecombinant ProteinsPlant ProteinsRecombinant Proteins

Identifiers

PMID29123155
PMCPMC5680255

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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.