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

The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America - 1 Aug 2000

Schwartz C J, Djaman O, Imlay J A, Kiley P J

Abstract excerpt

The cysteine desulfurase, IscS, provides sulfur for Fe-S cluster synthesis in vitro, but a role for IscS in in vivo Fe-S cluster formation has yet to be established. To study the in vivo function of IscS in Escherichia coli, a strain lacking IscS was constructed and characterized. Using this iscS deletion strain, we have observed decreased specific activities for proteins containing [4Fe-4S] clusters from soluble...

Read the complete abstract on PubMed

Topics

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

Share to Carbon-Sulfur Lyases
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Complementation Test

Share to Iron-Sulfur Proteins

Share to Mutation

Share to Niacin

Share to Phenotype

Share to Thiamine

Source

Open in PubMed Open full text

Identifiers

PMID: 10908675
DOI: 10.1073/pnas.160261497
PMCID: PMC16812

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli.PMID 10908675Read ↗

Lack of YggX results in chronic oxidative stress and uncovers subtle defects in Fe-S cluster metabolism in Salmonella enterica.Semantic proximity Read ↗

A connection between two ancient and essential cellular processes, iron-sulfur protein biogenesis and fatty acid synthesis, in <i>Escherichia coli</i>Semantic proximity Read ↗

Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo.Semantic proximity Read ↗

Repair of oxidized iron-sulfur clusters in Escherichia coli.Semantic proximity Read ↗

Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium.Semantic proximity Read ↗

Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems.Semantic proximity Read ↗

Novel features of the ISC machinery revealed by characterization of Escherichia coli mutants that survive without iron-sulfur clusters.Semantic proximity Read ↗

IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions.Semantic proximity Read ↗

Cysteine desulfurase (IscS)–mediated fine-tuning of bioenergetics and SUF expression prevents Mycobacterium tuberculosis hypervirulenceSemantic proximity Read ↗

[Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?].Semantic proximity Read ↗

Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis.Semantic proximity Read ↗

Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.Semantic proximity Read ↗

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