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

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

Molecular microbiology - 1 Mar 2001

Ralph E T, Scott C, Jordan P A, Thomson A J, Guest J R, Green J

Abstract excerpt

The FNR protein of Escherichia coli controls the transcription of target genes in response to anoxia. The anaerobic incorporation of oxygen-sensitive [4Fe 4S] clusters promotes dimerization, which in turn enhances DNA binding. Four potential iron ligands (C20, C23, C29 and C122) are essential for normal FNR activity in vivo. Three FNR variants (C20S, C23G and C29G) retained the ability to incorporate...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Anaerobiosis

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

Share to Dimerization

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Gene Expression Regulation, Bacterial

Share to Iron-Sulfur Proteins

Share to Models, Molecular

Source

Identifiers

PMID: 11251837
DOI: 10.1111/j.1365-2958.2001.02326.x

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

Anaerobic acquisition of [4FE 4S] clusters by the inactive FNR(C20S) variant and restoration of activity by second-site amino acid substitutions.PMID 11251837Read ↗

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

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

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

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

Substitution of leucine 28 with histidine in the Escherichia coli transcription factor FNR results in increased stability of the [4Fe-4S](2+) cluster to oxygen.Semantic proximity Read ↗

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

Defined inactive FecA derivatives mutated in functional domains of the outer membrane transport and signaling protein of Escherichia coli K-12.Semantic proximity Read ↗

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

Covalently linking the Escherichia coli global anaerobic regulator FNR in tandem allows it to function as an oxygen stable dimer.Semantic proximity Read ↗

Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants.Semantic proximity Read ↗

Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity.Semantic proximity Read ↗

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

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