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

H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing.

Nature structural & molecular biology - 1 May 2007

Bouffartigues Emeline, Buckle Malcolm, Badaut Cyril, Travers Andrew, Rimsky Sylvie

Abstract excerpt

H-NS is a protein of the bacterial nucleoid involved in DNA compaction and transcription regulation. In vivo, H-NS selectively silences specific genes of the bacterial chromosome. However, many studies have concluded that H-NS binds sequence-independently to DNA, leaving the molecular basis for its selectivity unexplained. We show that the negative regulatory element (NRE) of the supercoiling-sensitive...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA-Binding Proteins

Share to Gene Expression Regulation, Bacterial

Share to Gene Silencing

Share to Protein Binding

Share to Regulatory Elements, Transcriptional

Share to Transcription, Genetic

Source

Identifiers

PMID: 17435766
DOI: 10.1038/nsmb1233

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

H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing.PMID 17435766Read ↗

H-NS over-expression induces an artificial stationary phase by silencing global transcription.Semantic proximity Read ↗

Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS.Semantic proximity Read ↗

Nucleoprotein filament formation is the structural basis for bacterial protein H-NS gene silencing.Semantic proximity Read ↗

The chromatin-associated protein H-NS.Semantic proximity Read ↗

Promoter-specific repression of fimB expression by the Escherichia coli nucleoid-associated protein H-NS.Semantic proximity Read ↗

Phenotypic analysis of random hns mutations differentiate DNA-binding activity from properties of fimA promoter inversion modulation and bacterial motility.Semantic proximity Read ↗

Genetic Approaches to Study the Interplay Between Transcription and Nucleoid-Associated Proteins in Escherichia coli.Semantic proximity Read ↗

A truncated H-NS-like protein from enteropathogenic Escherichia coli acts as an H-NS antagonist.Semantic proximity Read ↗

Lack of the H-NS Protein Results in Extended and Aberrantly Positioned DNA during Chromosome Replication and Segregation in Escherichia coli.Semantic proximity Read ↗

Overexpression of the third H-NS paralogue H-NS2 compensates fitness loss in hns mutants of the enteroaggregative Escherichia coli strain 042.Semantic proximity Read ↗

The global regulator H-NS acts directly on the transpososome to promote Tn10 transposition.Semantic proximity Read ↗

The H-NS dimerization domain defines a new fold contributing to DNA recognition.Semantic proximity Read ↗

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