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

FNR-DNA interactions at natural and semi-synthetic promoters.

Molecular microbiology - 1 Jan 1996

Green J, Irvine A S, Meng W, Guest J R

Abstract excerpt

Two rapid and convenient methods have been developed for the amplification and purification of FNR, the anaerobic transcription regulator of Escherichia coli. The overproduced proteins resemble wild-type FNR in their basic properties: oligomeric state, iron contents (up to 2.7 atoms per monomer), DNA-binding affinities and ability to activate transcription. However, unlike previous preparations, FNR could be...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Binding Sites

Share to DNA-Binding Proteins

Share to Escherichia coli

Share to Genotype

Share to Molecular Sequence Data

Source

Identifiers

PMID: 8821942
DOI: 10.1046/j.1365-2958.1996.353884.x

Genes

CRP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FNR-DNA interactions at natural and semi-synthetic promoters.PMID 8821942Read ↗

In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E. coli.Semantic proximity Read ↗

DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen.Semantic proximity Read ↗

Repression of transcription initiation by Escherichia coli FNR protein: repression by FNR can be simple.Semantic proximity Read ↗

Regulation of aerobic-to-anaerobic transitions by the FNR cycle in Escherichia coli.Semantic proximity Read ↗

Miscoordination of the iron-sulfur clusters of the anaerobic transcription factor, FNR, allows simple repression but not activation.Semantic proximity Read ↗

Characterization of CprK1, a CRP/FNR-type transcriptional regulator of halorespiration from Desulfitobacterium hafniense.Semantic proximity Read ↗

Transcription activation by Escherichia coli FNR protein: similarities to, and differences from, the CRP paradigm.Semantic proximity Read ↗

Localization of upstream sequence elements required for nitrate and anaerobic induction of fdn (formate dehydrogenase-N) operon expression in Escherichia coli K-12.Semantic proximity Read ↗

Integration of three signals at the Escherichia coli nrf promoter: a role for Fis protein in catabolite repression.Semantic proximity Read ↗

Fine-tuned regulation by oxygen and nitric oxide of the activity of a semi-synthetic FNR-dependent promoter and expression of denitrification enzymes in Paracoccus denitrificans.Semantic proximity Read ↗

The function of isolated domains and chimaeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae.Semantic proximity Read ↗

Unusual organization, complexity and redundancy at the Escherichia coli hcp-hcr operon promoter.Semantic proximity Read ↗

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