Evidence map›Paper›PMID 26101259›Full record

ArticleNucleic acids research2015

Post-translational environmental switch of RadA activity by extein-intein interactions in protein splicing.

Natalya I Topilina, Olga Novikova, Matthew Stanger, Nilesh K Banavali, Marlene Belfort

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Conditional protein splicing of thebioRxiv : the preprint server for biology · 2024
    Article
  6. An intein-based biosensor to measure protein stability in vivo.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
  8. Review
  9. Journal of fungi (Basel, Switzerland) · 2022
    Article
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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

5 authors at 2 institutions in 1 country.

Natalya I TopilinaDepartment of Biological Sciences and RNA Institute, University at Albany, 1400 Washington Avenue, Albany, NY 12222, USA.
Olga NovikovaDepartment of Biological Sciences and RNA Institute, University at Albany, 1400 Washington Avenue, Albany, NY 12222, USA.
Matthew StangerDepartment of Biological Sciences and RNA Institute, University at Albany, 1400 Washington Avenue, Albany, NY 12222, USA.
Nilesh K BanavaliLaboratory of Computational and Structural Biology, Division of Genetics, Wadsworth Center, NYS Department of Health and Department of Biomedical Sciences, University at Albany, CMS 2008, Biggs Lab, Empire State Plaza, PO Box 509, Albany, NY 12201-2002, USA.
Marlene BelfortDepartment of Biological Sciences and RNA Institute, University at Albany, 1400 Washington Avenue, Albany, NY 12222, USA mbelfort@albany.edu.
University at Albany, State University of New York · USWadsworth Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational control based on an environmentally sensitive intervening intein sequence is described. Inteins are invasive genetic elements that self-splice at the protein level from the flanking host protein, the exteins. Here we show in Escherichia coli and in vitro that splicing of the RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. High temperature or solution conditions can unlock the intein for full activity, as can remote extein point mutations. Notably, this splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies coevolution of the parasitic intein and its host protein may provide a novel means of post-translational control.

Indexed as

ExteinsInteinsProtein SplicingArchaeal ProteinsBacterial ProteinsDNA-Binding ProteinsModels, MolecularMutationProtein Structure, SecondaryProtein Structure, TertiaryPyrococcus horikoshiiRec A RecombinasesTemperatureArchaeal ProteinsBacterial ProteinsDNA-Binding ProteinsRadA protein, archaealRadA protein, bacteriaRec A Recombinases

Identifiers

PMID26101259
PMCPMC4513877
OpenAlexW1651540401

What OpenQuestion holds

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LicenceCC BY-NC
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.