Evidence map›Paper›PMID 30169502›Full record

ArticlePloS one2018

VapC proteins from Mycobacterium tuberculosis share ribonuclease sequence specificity but differ in regulation and toxicity.

Abigail Sharrock, Alaine Ruthe, Emma S V Andrews, Vickery A Arcus, Joanna L Hicks

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Are all VapC toxins ofJournal of biosciences · 2024
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  9. Impact of Genomic Deletion RD16 on the Expression of theCurrent issues in molecular biology · 2023
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  10. DosR's multifaceted role onFrontiers in cellular and infection microbiology · 2023
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  12. Innate Immune Responses ofFrontiers in cellular and infection microbiology · 2021
    Article
  13. Article
  14. PhoH2 proteins couple RNA helicase and RNAse activities.Protein science : a publication of the Protein Society · 2020
    Review
  15. Review
  16. 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

5 authors at 1 institution in 1 country.

Abigail SharrockSchool of Science, University of Waikato, Hamilton, New Zealand.
Alaine RutheSchool of Science, University of Waikato, Hamilton, New Zealand.
Emma S V AndrewsSchool of Science, University of Waikato, Hamilton, New Zealand.
Vickery A ArcusSchool of Science, University of Waikato, Hamilton, New Zealand.
Joanna L HicksSchool of Science, University of Waikato, Hamilton, New Zealand.ORCID 0000-0002-0307-0923
University of Waikato · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chromosome of Mycobacterium tuberculosis (Mtb) contains a large number of Type II toxin-antitoxin (TA) systems. The majority of these belong to the VapBC TA family, characterised by the VapC protein consisting of a PIN domain with four conserved acidic residues, and proposed ribonuclease activity. Characterisation of five VapC (VapC1, 19, 27, 29 and 39) proteins from various regions of the Mtb chromosome using a combination of pentaprobe RNA sequences and mass spectrometry revealed a shared ribonuclease sequence-specificity with a preference for UAGG sequences. The TA complex VapBC29 is auto-regulatory and interacts with inverted repeat sequences in the vapBC29 promoter, whereas complexes VapBC1 and VapBC27 display no auto-regulatory properties. The difference in regulation could be due to the different properties of the VapB proteins, all of which belong to different VapB protein families. Regulation of the vapBC29 operon is specific, no cross-talk among Type II TA systems was observed. VapC29 is bacteriostatic when expressed in Mycobacterium smegmatis, whereas VapC1 and VapC27 displayed no toxicity upon expression in M. smegmatis. The shared sequence specificity of the five VapC proteins characterised is intriguing, we propose that the differences observed in regulation and toxicity is the key to understanding the role of these TA systems in the growth and persistence of Mtb.

Indexed as

AntitoxinsBacterial ProteinsBacterial ToxinsDNA-Binding ProteinsGene Expression Regulation, BacterialMycobacterium smegmatisMycobacterium tuberculosisOperonPromoter Regions, GeneticRibonucleasesAntitoxinsBacterial ProteinsBacterial ToxinsDNA-Binding ProteinsRibonucleases

Identifiers

PMID30169502
PMCPMC6118392
OpenAlexW2889543513

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.