Evidence map›Paper›PMID 18485078›Full record

ArticleMolecular microbiology2008

A basic/hydrophobic cleft of the T4 activator MotA interacts with the C-terminus of E.coli sigma70 to activate middle gene transcription.

Richard P Bonocora, Gregori Caignan, Christopher Woodrell, Milton H Werner, Deborah M Hinton

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Tevenvirinae phages encode a family of LSm-like fold proteins.Computational and structural biotechnology journal · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Structural basis of σ appropriation.Nucleic acids research · 2019
    Article
  7. A Novel Bvg-Repressed Promoter CausesJournal of bacteriology · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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  17. Review
  18. 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 4 institutions in 2 countries.

Richard P BonocoraGene Expression and Regulation Section, Laboratory of Molecular and Cellular Biology, NIDDK, National Institutes of Health, Bethesda, MD, USA.
Gregori Caignan
Christopher Woodrell
Milton H Werner
Deborah M Hinton
Rockefeller University · USIn-Q-Tel · USNational Institutes of Health · USZero to Three · US

Funding

Stuctural basis of polymerase recruitment to promotersR01GM063793 · NIGMS · ROCKEFELLER UNIVERSITY · PI WERNER, MILTON H. · 2001 to 2005
$1.3M
BACTERIOPHAGE T4 GENE EXPRESSIONZ01DK057802 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HINTON, DEBORAH M · 1993 to 2008
$599k
Intramural NIH HHS Z01 DK057802NIGMS NIH HHS 5R01GM063793-04NIGMS NIH HHS R01 GM063793
6 · The paper itself

Abstract

Transcriptional activation often employs a direct interaction between an activator and RNA polymerase. For activation of its middle genes, bacteriophage T4 appropriates Escherichia coli RNA polymerase through the action of two phage-encoded proteins, MotA and AsiA. Alone, AsiA inhibits transcription from a large class of host promoters by structurally remodelling region 4 of sigma(70), the primary specificity subunit of E. coli RNA polymerase. MotA interacts both with sigma(70) region 4 and with a DNA element present in T4 middle promoters. AsiA-induced remodelling is proposed to make the far C-terminus of sigma(70) region 4 accessible for MotA binding. Here, NMR chemical shift analysis indicates that MotA uses a 'basic/hydrophobic' cleft to interact with the C-terminus of AsiA-remodelled sigma(70), but MotA does not interact with AsiA itself. Mutations within this cleft, at residues K3, K28 and Q76, both impair the interaction of MotA with sigma(70) region 4 and MotA-dependent activation. Furthermore, mutations at these residues greatly decrease phage viability. Most previously described activators that target sigma(70) directly use acidic residues to engage a basic surface of region 4. Our work supports accumulated evidence indicating that 'sigma appropriation' by MotA and AsiA uses a fundamentally different mechanism to activate transcription.

Indexed as

Protein Interaction MappingTranscription, GeneticAmino Acid SequenceArtificial Gene FusionBacteriophage T4beta-GalactosidaseDNA-Binding ProteinsDNA-Directed RNA PolymerasesElectrophoretic Mobility Shift AssayEscherichia coliGenes, ReporterGenetic Complementation TestMagnetic Resonance SpectroscopyMicrobial ViabilityModels, MolecularMolecular Sequence DataAsiA protein, Enterobacteria phage T4beta-GalactosidaseDNA-Binding ProteinsDNA-Directed RNA PolymerasesMotA protein, Enterobacteria phage T4RNA polymerase sigma 70Sigma FactorTranscription FactorsViral Proteins

Identifiers

PMID18485078
PMCPMC2631437
OpenAlexW2113938608

What OpenQuestion holds

Textmetadata
LicenceTDM
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.