Evidence map›Paper›PMID 25123661›Full record

ArticleNucleic acids research2014

A high security double lock and key mechanism in HUH relaxases controls oriT-processing for plasmid conjugation.

José Daniel Carballeira, Blanca González-Pérez, Gabriel Moncalián, Fernando de la Cruz

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Frontiers in microbiology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Quorum Sensing N-acyl Homoserine Lactones-SdiA SuppressesFrontiers in cellular and infection microbiology · 2017
    Article
  12. Article
  13. 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

4 authors at 2 institutions in 1 country.

José Daniel CarballeiraDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC, Universidad de Cantabria-CSIC, C/Albert Einstein 22, 39011 Santander, Spain.
Blanca González-PérezDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC, Universidad de Cantabria-CSIC, C/Albert Einstein 22, 39011 Santander, Spain.
Gabriel MoncaliánDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC, Universidad de Cantabria-CSIC, C/Albert Einstein 22, 39011 Santander, Spain moncalig@unican.es.
Fernando de la CruzDepartamento de Biología Molecular e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC, Universidad de Cantabria-CSIC, C/Albert Einstein 22, 39011 Santander, Spain moncalig@unican.es.
Instituto de Biomedicina y Biotecnología de Cantabria · ESUniversidad de Cantabria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Relaxases act as DNA selection sieves in conjugative plasmid transfer. Most plasmid relaxases belong to the HUH endonuclease family. TrwC, the relaxase of plasmid R388, is the prototype of the HUH relaxase family, which also includes TraI of plasmid F. In this article we demonstrate that TrwC processes its target nic-site by means of a highly secure double lock and key mechanism. It is controlled both by TrwC-DNA intermolecular interactions and by intramolecular DNA interactions between several nic nucleotides. The sequence specificity map of the interaction between TrwC and DNA was determined by systematic mutagenesis using degenerate oligonucleotide libraries. The specificity map reveals the minimal nic sequence requirements for R388-based conjugation. Some nic-site sequence variants were still able to form the U-turn shape at the nic-site necessary for TrwC processing, as observed by X-ray crystallography. Moreover, purified TrwC relaxase effectively cleaved ssDNA as well as dsDNA substrates containing these mutant sequences. Since TrwC is able to catalyze DNA integration in a nic-site-containing DNA molecule, characterization of nic-site functionally active sequence variants should improve the search quality of potential target sequences for relaxase-mediated integration in any target genome.

Indexed as

Conjugation, GeneticCatalytic DomainDNA, BacterialDNA NucleotidyltransferasesDNA, Single-StrandedGene LibraryMutationPlasmidsDNA, BacterialDNA NucleotidyltransferasesDNA relaxaseDNA, Single-Stranded

Identifiers

PMID25123661
PMCPMC4176350
OpenAlexW2104378409

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.