Evidence map›Paper›PMID 34898262›Full record

ArticleJournal of bacteriology2022

Development of a Highly Sensitive Luciferase-Based Reporter System To Study Two-Step Protein Secretion in Cyanobacteria.

David A Russo, Julie A Z Zedler, Fabian D Conradi, Nils Schuergers, Poul Erik Jensen, Conrad W Mullineaux, Annegret Wilde, Georg Pohnert

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

David A RussoBioorganic Analytics, Institute for Inorganic and Analytical Chemistry, Friedrich Schiller University Jenagrid.9613.d, Jena, Germany.ORCID 0000-0002-4729-1701
Julie A Z ZedlerMatthias Schleiden Institute for Genetics, Bioinformatics and Molecular Botany, Friedrich Schiller University Jenagrid.9613.d, Jena, Germany.ORCID 0000-0002-0462-8810
Fabian D ConradiSchool of Biological and Behavioural Sciences, Queen Mary University of London, London, United Kingdom.
Nils SchuergersMolecular Genetics of Prokaryotes, Institute of Biology III, University of Freiburggrid.5963.9, Freiburg, Germany.ORCID 0000-0002-8703-9519
Poul Erik JensenDepartment of Food Science, University of Copenhagen, Frederiksberg, Denmark.ORCID 0000-0001-6524-7723
Conrad W MullineauxSchool of Biological and Behavioural Sciences, Queen Mary University of London, London, United Kingdom.ORCID 0000-0001-7194-9916
Annegret WildeMolecular Genetics of Prokaryotes, Institute of Biology III, University of Freiburggrid.5963.9, Freiburg, Germany.ORCID 0000-0003-0935-8415
Georg PohnertBioorganic Analytics, Institute for Inorganic and Analytical Chemistry, Friedrich Schiller University Jenagrid.9613.d, Jena, Germany.ORCID 0000-0003-2351-6336
Friedrich Schiller University Jena · DEQueen Mary University of London · GBUniversity of Freiburg · DEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyanobacteria, ubiquitous oxygenic photosynthetic bacteria, interact with the environment and their surrounding microbiome through the secretion of a variety of small molecules and proteins. The release of these compounds is mediated by sophisticated multiprotein complexes, also known as secretion systems. Genomic analyses indicate that protein and metabolite secretion systems are widely found in cyanobacteria; however, little is known regarding their function, regulation, and secreted effectors. One such system, the type IVa pilus system (T4aPS), is responsible for the assembly of dynamic cell surface appendages, type IVa pili (T4aP), that mediate ecologically relevant processes such as phototactic motility, natural competence, and adhesion. Several studies have suggested that the T4aPS can also act as a two-step protein secretion system in cyanobacteria akin to the homologous type II secretion system in heterotrophic bacteria. To determine whether the T4aP are involved in two-step secretion of nonpilin proteins, we developed a NanoLuc (NLuc)-based quantitative secretion reporter for the model cyanobacterium

Indexed as

Bacterial ProteinsBiological AssayFimbriae, BacterialLuciferasesProtein Translocation SystemsProtein TransportSynechocystisBacterial ProteinsLuciferasesnanolucProtein Translocation Systemscyanobacteriageneral secretory pathwayNanoLuc luciferaseprotein secretionSynechocystistype IV pili

Identifiers

PMID34898262
PMCPMC8846455
OpenAlexW4220775030

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.