Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure of bacterial regulatory RNAs determines their performance in competition for the chaperone protein Hfq.

Biochemistry - 10 Feb 2015

Małecka Ewelina M, Stróżecka Joanna, Sobańska Daria, Olejniczak Mikołaj

Abstract excerpt

Bacterial regulatory RNAs require the chaperone protein Hfq to enable their pairing to mRNAs. Recent data showed that there is a hierarchy among sRNAs in the competition for access to Hfq, which could be important for the tuning of sRNA-dependent translation regulation. Here, seven structurally different sRNAs were compared using filter-based competition assays. Moreover, chimeric sRNA constructs were designed to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Host Factor 1 Protein

Share to Molecular Chaperones

Share to Nucleic Acid Conformation

Share to Protein Binding

Share to RNA, Bacterial

Share to RNA, Untranslated

Source

Identifiers

PMID: 25582129
DOI: 10.1021/bi500741d

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of bacterial regulatory RNAs determines their performance in competition for the chaperone protein Hfq.PMID 25582129Read ↗

The binding of Class II sRNA MgrR to two different sites on matchmaker protein Hfq enables efficient competition for Hfq and annealing to regulated mRNAs.Semantic proximity Read ↗

The functional Hfq-binding module of bacterial sRNAs consists of a double or single hairpin preceded by a U-rich sequence and followed by a 3' poly(U) tail.Semantic proximity Read ↗

Mutations in interaction surfaces differentially impact E. coli Hfq association with small RNAs and their mRNA targets.Semantic proximity Read ↗

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

Acidic Residues in the Hfq Chaperone Increase the Selectivity of sRNA Binding and Annealing.Semantic proximity Read ↗

Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites.Semantic proximity Read ↗

Major role for mRNA binding and restructuring in sRNA recruitment by Hfq.Semantic proximity Read ↗

The RNA binding protein Hfq interacts specifically with tRNAs.Semantic proximity Read ↗

Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function.Semantic proximity Read ↗

The stoichiometry of the Escherichia coli Hfq protein bound to RNA.Semantic proximity Read ↗

New molecular interactions broaden the functions of the RNA chaperone HfqSemantic proximity Read ↗

Conserved arginines on the rim of Hfq catalyze base pair formation and exchange.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.