Evidence map›Paper›PMID 18366439›Full record

ArticleMolecular microbiology2008

Differences in the mechanism of the allosteric l-rhamnose responses of the AraC/XylS family transcription activators RhaS and RhaR.

Ana Kolin, Vinitha Balasubramaniam, Jeff M Skredenske, Jason R Wickstrum, Susan M Egan

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

19 citing papers in PubMed, 22 citations in OpenAlex.

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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 3 institutions in 1 country.

Ana KolinDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS, USA.
Vinitha Balasubramaniam
Jeff M Skredenske
Jason R Wickstrum
Susan M Egan
University of Kansas · USUniformed Services University of the Health Sciences · USUniversity of Kansas Medical Center · US

Funding

TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI FISCHER, CHRISTOPHER JAMES · 2002 to 2011
$20.1M
Transcription Activation at the rhaBAD OperonR01GM055099 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI EGAN, SUSAN M · 2005 to 2008
$820k
TRANSCRIPTION ACTIVATION AT THE RHABAD OPERONR29GM055099 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI EGAN, SUSAN M · 1997 to 2001
$215k
NCRR NIH HHS P20 RR017708NCRR NIH HHS P20 RR17708NIGMS NIH HHS GM55099NIGMS NIH HHS R01 GM055099NIGMS NIH HHS R29 GM055099
6 · The paper itself

Abstract

Proteins in the largest subset of AraC/XylS family transcription activators, including RhaS and RhaR, have C-terminal domains (CTDs) that mediate DNA-binding and transcription activation, and N-terminal domains (NTDs) that mediate dimerization and effector binding. The mechanism of the allosteric effector response in this family has been identified only for AraC. Here, we investigated the mechanism by which RhaS and RhaR respond to their effector, l-rhamnose. Unlike AraC, N-terminal truncations suggested that RhaS and RhaR do not use an N-terminal arm to inhibit activity in the absence of effector. We used random mutagenesis to isolate RhaS and RhaR variants with enhanced activation in the absence of l-rhamnose. NTD substitutions largely clustered around the predicted l-rhamnose-binding pockets, suggesting that they mimic the structural outcome of effector binding to the wild-type proteins. RhaS-CTD substitutions clustered in the first HTH motif, and suggested that l-rhamnose induces improved DNA binding. In contrast, RhaR-CTD substitutions clustered at a single residue in the second HTH motif, at a position consistent with improved RNAP contacts. We propose separate allosteric mechanisms for the two proteins: Without l-rhamnose, RhaS does not effectively bind DNA while RhaR does not effectively contact RNAP. Upon l-rhamnose binding, both proteins undergo structural changes that enable transcription activation.

Indexed as

Amino Acid SubstitutionArtificial Gene Fusionbeta-GalactosidaseBinding SitesDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGenes, ReporterModels, BiologicalModels, MolecularMutagenesis, Site-DirectedMutation, MissenseRhamnoseSequence DeletionTrans-ActivatorsTranscriptional Activationbeta-GalactosidaseDNA-Binding ProteinsEscherichia coli ProteinsRhamnoseRhaR protein, E coliRhaS protein, E coliTrans-Activators

Identifiers

PMID18366439
PMCPMC2377013
OpenAlexW1846768462

What OpenQuestion holds

Textmetadata
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.