Evidence map›Paper›PMID 19767437›Full record

ArticleJournal of bacteriology2009

Plasmid r1 conjugative DNA processing is regulated at the coupling protein interface.

Sanja Mihajlovic, Silvia Lang, Marta V Sut, Heimo Strohmaier, Christian J Gruber, Günther Koraimann, Elena Cabezón, Gabriel Moncalián, Fernando de la Cruz, Ellen L Zechner

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  13. Article
  14. Structures of TraI in solution.Journal of molecular modeling · 2014
    Article
  15. Article
  16. Article
  17. Article
  18. Assembly and mechanisms of bacterial type IV secretion machines.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  19. Article
  20. 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

10 authors at 3 institutions in 2 countries.

Sanja MihajlovicUniversity of Graz, Institute of Molecular Biosciences, Humboldtstrasse 50, A-8010 Graz, Austria.
Silvia Lang
Marta V Sut
Heimo Strohmaier
Christian J Gruber
Günther Koraimann
Elena Cabezón
Gabriel Moncalián
Fernando de la Cruz
Ellen L Zechner
University of Graz · ATUniversidad de Cantabria · ESInstituto de Biomedicina y Biotecnología de Cantabria · ES

Funding

Austrian Science Fund FWF P 18607Austrian Science Fund FWF W 901
6 · The paper itself

Abstract

Selective substrate uptake controls initiation of macromolecular secretion by type IV secretion systems in gram-negative bacteria. Type IV coupling proteins (T4CPs) are essential, but the molecular mechanisms governing substrate entry to the translocation pathway remain obscure. We report a biochemical approach to reconstitute a regulatory interface between the plasmid R1 T4CP and the nucleoprotein relaxosome dedicated to the initiation stage of plasmid DNA processing and substrate presentation. The predicted cytosolic domain of T4CP TraD was purified in a predominantly monomeric form, and potential regulatory effects of this protein on catalytic activities exhibited by the relaxosome during transfer initiation were analyzed in vitro. TraDDeltaN130 stimulated the TraI DNA transesterase activity apparently via interactions on both the protein and the DNA levels. TraM, a protein interaction partner of TraD, also increased DNA transesterase activity in vitro. The mechanism may involve altered DNA conformation as TraM induced underwinding of oriT plasmid DNA in vivo (DeltaL(k) = -4). Permanganate mapping of the positions of duplex melting due to relaxosome assembly with TraDDeltaN130 on supercoiled DNA in vitro confirmed localized unwinding at nic but ruled out formation of an open complex compatible with initiation of the TraI helicase activity. These data link relaxosome regulation to the T4CP and support the model that a committed step in the initiation of DNA export requires activation of TraI helicase loading or catalysis.

Indexed as

Bacterial ProteinsDNA, BacterialDNA-Binding ProteinsDNA HelicasesElectrophoresis, Agar GelElectrophoresis, Gel, Two-DimensionalEscherichia coli ProteinsMass SpectrometryMembrane ProteinsPlasmidsProtein BindingBacterial ProteinsDNA, BacterialDNA-Binding ProteinsDNA HelicasesEscherichia coli ProteinsMembrane ProteinstraD protein, E coliTraI protein, E coli

Identifiers

PMID19767437
PMCPMC2772491
OpenAlexW2027916691

What OpenQuestion holds

Textmetadata
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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.