Evidence map›Paper›PMID 7568139›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

The amino-terminal domain of the prokaryotic enhancer-binding protein XylR is a specific intramolecular repressor.

J Pérez-Martín, V De Lorenzo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Review
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  9. Bacterial transcriptional regulators for degradation pathways of aromatic compounds.Microbiology and molecular biology reviews : MMBR · 2004
    Review
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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

2 authors.

J Pérez-MartínCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
V De Lorenzo

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism under which the signal-reception amino-terminal portion (A domain) of the prokaryotic enhancer-binding protein XylR controls the activity of the regulator has been investigated through complementation tests in vivo, in which the various protein segments were produced as independent polypeptides. Separate expression of the A domain repressed the otherwise constitutive activity of a truncated derivative of XylR deleted of its A domain (XylR delta A). Such inhibition was not released by m-xylene, the natural inducer of the system. Repression caused by the A domain was specific for XylR because it did not affect activation of the sigma 54 promoter PnifH by a derivative of its cognate regulator, NifA, deleted of its own A domain. The A domain was also unable to repress the activity of a NifA-XylR hybrid protein resulting from fusing two-thirds of the central domain of NifA to the carboxyl-terminal third of XylR, which includes its DNA-binding domain. The inhibitory effect caused by the A domain of XylR on XylR delta A seems, therefore, to result from specific interactions in trans between the two truncated proteins and not from mere hindering of an activating surface.

Indexed as

DNA-Binding ProteinsEnhancer Elements, GeneticBacterial ProteinsBinding SitesEscherichia coliIsopropyl ThiogalactosideModels, StructuralPeptide FragmentsPromoter Regions, GeneticRecombinant Fusion ProteinsRepressor ProteinsTranscription FactorsXylenes3-xyleneBacterial ProteinsDNA-Binding ProteinsIsopropyl ThiogalactosideNifA protein, BacteriaPeptide FragmentsRecombinant Fusion ProteinsRepressor ProteinsTranscription FactorsXylenesXylR protein, Pseudomonas

Identifiers

PMID7568139
PMCPMC40991

What OpenQuestion holds

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Registered trials

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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.