Evidence map›Paper›PMID 15342598›Full record

ArticleJournal of bacteriology2004

Amino acid contacts between sigma 70 domain 4 and the transcription activators RhaS and RhaR.

Jason R Wickstrum, Susan M Egan

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Fructose-1-kinase has pleiotropic roles inbioRxiv : the preprint server for biology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Jason R WickstrumDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Susan M Egan
University of Kansas · 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 RR-P20 RR17708NIGMS NIH HHS GM55099NIGMS NIH HHS R01 GM055099NIGMS NIH HHS R29 GM055099
6 · The paper itself

Abstract

The RhaS and RhaR proteins are transcription activators that respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. RhaR activates transcription of rhaSR, and RhaS activates transcription of the operon that encodes the L-rhamnose catabolic enzymes, rhaBAD, as well as the operon that encodes the L-rhamnose transport protein, rhaT. RhaS is 30% identical to RhaR at the amino acid level, and both are members of the AraC/XylS family of transcription activators. The RhaS and RhaR binding sites overlap the -35 hexamers of the promoters they regulate, suggesting they may contact the sigma70 subunit of RNA polymerase as part of their mechanisms of transcription activation. In support of this hypothesis, our lab previously identified an interaction between RhaS residue D241 and sigma70 residue R599. In the present study, we first identified two positively charged amino acids in sigma70, K593 and R599, and three negatively charged amino acids in RhaR, D276, E284, and D285, that were important for RhaR-mediated transcription activation of the rhaSR operon. Using a genetic loss-of-contact approach we have obtained evidence for a specific contact between RhaR D276 and sigma70 R599. Finally, previous results from our lab separately showed that RhaS D250A and sigma70 K593A were defective at the rhaBAD promoter. Our genetic loss-of-contact analysis of these residues indicates that they identify a second site of contact between RhaS and sigma70.

Indexed as

Protein Interaction MappingAmino Acid SequenceAmino Acid SubstitutionArtificial Gene Fusionbeta-GalactosidaseDNA-Binding ProteinsDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsGenes, ReporterModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutation, MissenseSigma FactorTrans-Activatorsbeta-GalactosidaseDNA-Binding ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsRhaR protein, E coliRhaS protein, E coliRNA polymerase sigma 70Sigma FactorTrans-Activators

Identifiers

PMID15342598
PMCPMC515164
OpenAlexW2156521865

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.