Evidence map›Paper›PMID 32024928›Full record

ArticleScientific reports2020

Identification and characterization of novel filament-forming proteins in cyanobacteria.

Benjamin L Springstein, Christian Woehle, Julia Weissenbach, Andreas O Helbig, Tal Dagan, Karina Stucken

Abstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The cyanobacterial taxis protein HmpF regulates type IV pilus activity in response to light.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Review
  12. A bacterial cytolinker couples positioning of magnetic organelles to cell shape control.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

6 authors.

Benjamin L SpringsteinInstitute of General Microbiology, Christian-Albrechts-Universität zu Kiel, Kiel, Germany. benjamin_springstein@hms.harvard.edu.ORCID http://orcid.org/0000-0002-3461-5391
Christian WoehleInstitute of General Microbiology, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.
Julia WeissenbachInstitute of General Microbiology, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.
Andreas O HelbigInstitute for Experimental Medicine, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.
Tal DaganInstitute of General Microbiology, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.ORCID http://orcid.org/0000-0002-9042-192X
Karina StuckenDepartment of Food Engineering, Universidad de La Serena, La Serena, Chile. kstucken@userena.cl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filament-forming proteins in bacteria function in stabilization and localization of proteinaceous complexes and replicons; hence they are instrumental for myriad cellular processes such as cell division and growth. Here we present two novel filament-forming proteins in cyanobacteria. Surveying cyanobacterial genomes for coiled-coil-rich proteins (CCRPs) that are predicted as putative filament-forming proteins, we observed a higher proportion of CCRPs in filamentous cyanobacteria in comparison to unicellular cyanobacteria. Using our predictions, we identified nine protein families with putative intermediate filament (IF) properties. Polymerization assays revealed four proteins that formed polymers in vitro and three proteins that formed polymers in vivo. Fm7001 from Fischerella muscicola PCC 7414 polymerized in vitro and formed filaments in vivo in several organisms. Additionally, we identified a tetratricopeptide repeat protein - All4981 - in Anabaena sp. PCC 7120 that polymerized into filaments in vitro and in vivo. All4981 interacts with known cytoskeletal proteins and is indispensable for Anabaena viability. Although it did not form filaments in vitro, Syc2039 from Synechococcus elongatus PCC 7942 assembled into filaments in vivo and a Δsyc2039 mutant was characterized by an impaired cytokinesis. Our results expand the repertoire of known prokaryotic filament-forming CCRPs and demonstrate that cyanobacterial CCRPs are involved in cell morphology, motility, cytokinesis and colony integrity.

Indexed as

Amino Acid MotifsAnabaenaBacterial ProteinsCyanobacteriaCytoskeletal ProteinsCytoskeletonGenes, BacterialMutationProtein Conformation, alpha-HelicalProtein MultimerizationRecombinant ProteinsSynechococcusBacterial ProteinsCytoskeletal ProteinsRecombinant Proteins

Identifiers

PMID32024928
PMCPMC7002697

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.