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

In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E. coli.

FEBS letters - 17 Sept 1990

Sharrocks A D, Green J, Guest J R

Abstract excerpt

FNR regulates the expression of target genes in response to anaerobiosis. It resembles the catabolite gene activator or cAMP-receptor protein (CRP) except for the presence of an N-terminal cysteine cluster, which may form a redox-sensing iron-binding site. Site-directed mutagenesis has shown that 3 of the 4 cysteine residues in the N-terminal cluster (Cys-20, -23 and -29, but not Cys-16) and the only other...

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 DNA-Binding Proteins

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Share to Transcription Factors

Source

Identifiers

PMID: 2226775
DOI: 10.1016/0014-5793(90)81248-m

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

In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E. coli.PMID 2226775Read ↗

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

Transcription activation by FNR: evidence for a functional activating region 2.Semantic proximity Read ↗

Anaerobic acquisition of [4FE 4S] clusters by the inactive FNR(C20S) variant and restoration of activity by second-site amino acid substitutions.Semantic proximity Read ↗

FNR-DNA interactions at natural and semi-synthetic promoters.Semantic proximity Read ↗

Characterization of activating region 3 from Escherichia coli FNR.Semantic proximity Read ↗

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

Characterization of FNR* mutant proteins indicates two distinct mechanisms for altering oxygen regulation of the Escherichia coli transcription factor FNR.Semantic proximity Read ↗

In vitro analysis of a constitutively active mutant form of the Escherichia coli global transcription factor FNR.Semantic proximity Read ↗

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

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

Dissecting the role of the N-terminal region of the Escherichia coli global transcription factor FNR.Semantic proximity Read ↗

The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state.Semantic proximity Read ↗

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