Evidence map›Paper›PMID 29322483›Full record

ArticlePhotosynthesis research2018

Structural integrity of Synechocystis sp. PCC 6803 phycobilisomes evaluated by means of differential scanning calorimetry.

Nia Petrova, Svetla Todinova, Hajnalka Laczko-Dobos, Tomas Zakar, Sindhujaa Vajravel, Stefka Taneva, Zoltan Gombos, Sashka Krumova

Abstract read
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In one paragraph

Article in Photosynthesis research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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 2 countries.

Nia PetrovaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Bl. 21, 1113, Sofia, Bulgaria.
Svetla TodinovaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Bl. 21, 1113, Sofia, Bulgaria.
Hajnalka Laczko-DobosInstitute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged, 6726, Hungary.ORCID http://orcid.org/0000-0002-8962-376X
Tomas ZakarInstitute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged, 6726, Hungary.
Sindhujaa VajravelInstitute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged, 6726, Hungary.
Stefka TanevaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Bl. 21, 1113, Sofia, Bulgaria.
Zoltan GombosInstitute of Plant Biology, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, Szeged, 6726, Hungary.ORCID http://orcid.org/0000-0003-4031-009X
Sashka KrumovaInstitute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Bl. 21, 1113, Sofia, Bulgaria. sakrumo@gmail.com.ORCID http://orcid.org/0000-0001-7412-8398
Bulgarian Academy of Sciences · BGHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

Bulgarian Academy of Sciences bilateral collaboration between the Bulgarian and Hungarian Academy of SciencesHungarian Government Grant GINOP-2.3.2-15-2016-00001Hungarian Scientific Research Fund K108411Hungarian Scientific Research Fund PD10855
6 · The paper itself

Abstract

Phycobilisomes (PBSs) are supramolecular pigment-protein complexes that serve as light-harvesting antennae in cyanobacteria. They are built up by phycobiliproteins assembled into allophycocyanin core cylinders (ensuring the physical interaction with the photosystems) and phycocyanin rods (protruding from the cores and having light-harvesting function), the whole PBSs structure being maintained by linker proteins. PBSs play major role in light-harvesting optimization in cyanobacteria; therefore, the characterization of their structural integrity in intact cells is of great importance. The present study utilizes differential scanning calorimetry and spectroscopy techniques to explore for the first time, the thermodynamic stability of PBSs in intact Synechocystis sp. PCC 6803 cells and to probe its alteration as a result of mutations or under different growth conditions. As a first step, we characterize the thermodynamic behavior of intact and dismantled PBSs isolated from wild-type cells (having fully assembled PBSs) and from CK mutant cells (that lack phycocyanin rods and contain only allophycocyanin cores), and identified the thermal transitions of phycocyanin and allophycocyanin units in vitro. Next, we demonstrate that in intact cells PBSs exhibit sharp, high amplitude thermal transition at about 63 °C that strongly depends on the structural integrity of the PBSs supercomplex. Our findings implicate that calorimetry could offer a valuable approach for the assessment of the influence of variety of factors affecting the stability and structural organization of phycobilisomes in intact cyanobacterial cells.

Indexed as

Calorimetry, Differential ScanningMutationPhycobilisomesSynechocystisThermodynamicsPhycobilisomesCyanobacterial mutantsDifferential scanning calorimetryPhycobilisomesSynechocystis sp. PCC 6803Thermal stability

Identifiers

PMID29322483
OpenAlexW2783289784

What OpenQuestion holds

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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.