An In Vivo Method for Characterization of Protein Interactions within Sulfur Trafficking Systems of E. coli (Q33714924)

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scientific article published on November 2, 2010

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English	An In Vivo Method for Characterization of Protein Interactions within Sulfur Trafficking Systems of E. coli	scientific article published on November 2, 2010

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scholarly article

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Europe PubMed Central

PubMed publication ID

20936830

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28 July 2017

title

An in vivo method for characterization of protein interactions within sulfur trafficking systems of E. coli (English)

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Europe PubMed Central

PubMed publication ID

20936830

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28 July 2017

An In Vivo Method for Characterization of Protein Interactions within Sulfur Trafficking Systems of E. coli (English)

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Crossref

DOI

10.1021/PR100920R

reference URL

https://api.crossref.org/works/10.1021/PR100920R

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31 July 2024

main subject

Escherichia coli

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author name string

Heather M. Bolstad

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1

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Europe PubMed Central

PubMed publication ID

20936830

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Matthew J. Wood

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2

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Europe PubMed Central

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20936830

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31 July 2024

language of work or name

English

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National Center for Biotechnology Information

PubMed publication ID

20936830

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=20936830

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31 July 2024

publication date

2 November 2010

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PubMed publication ID

20936830

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28 July 2017

full work available at URL

https://pubs.acs.org/doi/pdf/10.1021/pr100920r

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Crossref

DOI

10.1021/PR100920R

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https://api.crossref.org/works/10.1021/PR100920R

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31 July 2024

published in

Journal of Proteome Research

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Europe PubMed Central

PubMed publication ID

20936830

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28 July 2017

volume

9

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Europe PubMed Central

PubMed publication ID

20936830

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28 July 2017

issue

12

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Europe PubMed Central

PubMed publication ID

20936830

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28 July 2017

page(s)

6740-6751

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Europe PubMed Central

PubMed publication ID

20936830

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28 July 2017

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The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli.

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Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: evidence for its implication in the pathogen's survival

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Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)

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Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli

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The redox-switch domain of Hsp33 functions as dual stress sensor

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Identification of a redox-regulated chaperone network

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NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions

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Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.

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Monothiol glutaredoxins: a common domain for multiple functions.

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Glutaredoxins: roles in iron homeostasis

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Enterobactin: an archetype for microbial iron transport

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Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography

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Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role

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Iron-sulphur clusters and the problem with oxygen

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The generation of 5′-deoxyadenosyl radicals by adenosylmethionine-dependent radical enzymes

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Structure, function, and formation of biological iron-sulfur clusters

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Inactivation of Dehydratase [4Fe-4S] Clusters and Disruption of Iron Homeostasis upon Cell Exposure to Peroxynitrite

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Ironminus signSulfur Proteins with Nonredox Functions

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MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters.

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The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase

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Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli.

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Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion

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Siderophore-controlled iron assimilation in the enterobacterium Erwinia chrysanthemi: evidence for the involvement of bacterioferritin and the Suf iron-sulfur cluster assembly machinery

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

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Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families

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Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate

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Iron-sulfur cluster biosynthesis

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Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin

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CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster

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Protein abundance profiling of the Escherichia coli cytosol

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High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases

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

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Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.

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The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H

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The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD

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Proteomic Analysis of Protein−Protein Interactions within the Cysteine Sulfinate Desulfinase Fe−S Cluster Biogenesis System

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31 July 2024

Identifiers

DOI

10.1021/PR100920R

1 reference

stated in

Europe PubMed Central

PubMed publication ID

20936830

retrieved

28 July 2017

PubMed publication ID

20936830

1 reference

stated in

Europe PubMed Central

PubMed publication ID

20936830

retrieved

28 July 2017

 

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