Evidence map›Paper›PMID 15531892›Full record

ArticleNature structural & molecular biology2004

Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs.

Peter J Mikulecky, Meenakshi K Kaw, Cristin C Brescia, Jennifer C Takach, Darren D Sledjeski, Andrew L Feig

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

148 citing papers in PubMed, 251 citations in OpenAlex.

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  8. Competition for Hfq drives kinetic selection of mRNA targets byProceedings of the National Academy of Sciences of the United States of America · 2025
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  18. Specific and Global RNA Regulators inInternational journal of molecular sciences · 2021
    Review
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88 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Peter J MikuleckyDepartment of Chemistry, Indiana University, 800 E. Kirkwood Avenue, Bloomington, Indiana 47405, USA.
Meenakshi K Kaw
Cristin C Brescia
Jennifer C Takach
Darren D Sledjeski
Andrew L Feig
Indiana University Bloomington · USUniversity of Toledo Medical Center · US

Funding

TRAINING IN GENETICST32GM007757 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI KUMAR, JUSTIN P · 1985 to 2014
$8.1M
RNA Cold DenaturationR01GM065430 · NIGMS · WAYNE STATE UNIVERSITY · PI FEIG, ANDREW L · 2003 to 2007
$1.1M
Investigations of Hfq-RNA InteractionsR01GM075068 · NIGMS · WAYNE STATE UNIVERSITY · PI FEIG, ANDREW L · 2005 to 2008
$931k
REGULATION BY THE ESCHERICHIA COLI SMALL RNA, DSRAR01GM056448 · NIGMS · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI SLEDJESKI, DARREN D. · 1998 to 2002
$431k
NIGMS NIH HHS GM056448NIGMS NIH HHS GM065430NIGMS NIH HHS R01 GM065430NIGMS NIH HHS R01 GM075068NIGMS NIH HHS T32 GM007757NIGMS NIH HHS T32-GM07757
6 · The paper itself

Abstract

The bacterial Sm-like protein Hfq facilitates RNA-RNA interactions involved in post-transcriptional regulation of the stress response. Specifically, Hfq helps pair noncoding RNAs (ncRNAs) with complementary regions of target mRNAs. To probe the mechanism of this pairing, we generated a series of Hfq mutants and measured their affinity for RNAs like those with which Hfq must associate in vivo. We tested the mutants' DsrA-dependent activation of rpoS, and their ability to stabilize DsrA ncRNA against degradation in vivo. Our results suggest that Hfq has two independent RNA-binding surfaces. In addition to a well-known site around the core of the Hfq hexamer, we observe interactions with the distal face of Hfq, a new locus with which mRNAs and poly(A) sequences associate. Our model explains how Hfq can simultaneously bind a ncRNA and its mRNA target to facilitate the strand displacement reaction required for Hfq-dependent translational regulation.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsBinding, CompetitiveCalorimetryEscherichia coliEscherichia coli ProteinsHost Factor 1 ProteinModels, MolecularMolecular Sequence DataMutationPoly AProtein DenaturationProtein Structure, TertiaryRNA-Binding ProteinsRNA, MessengerBacterial Outer Membrane ProteinsBacterial ProteinsDrsA protein, E coliEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinPoly ARNA-Binding ProteinsRNA, MessengerSigma Factorsigma factor KatF protein, Bacteria

Identifiers

PMID15531892
PMCPMC3071270
OpenAlexW2093748687

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.