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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-2-9
pubmed:databankReference
pubmed:abstractText
During a search for genes encoding electron transport proteins from a Thiobacillus ferroxidans ATCC 33020 gene bank, a 19.8 kb plasmid, pTF5, which conferred increased sensitivity to the antimicrobial agent metronidazole upon an Escherichia coli mutant, was isolated and cloned in E. coli. The plasmid had an identical restriction enzyme map to a plasmid which has been found in T. ferrooxidans strains isolated from many different parts of the world. The plasmid was present at between two and four copies per genome and contained a region of approximately 5-6 kb which was also found on the chromosome. This region was sequenced and found to have four complete ORFs, which when translated had high percentage amino acid similarity to [3Fe-4S,4Fe-4S] ferredoxins, proteins of the FNR regulator family, prismane-like proteins and the NADH oxidoreductase subunit of a methane monooxygenase. In vitro protein analysis using an E. coli-derived transcription-translation system indicated that three of the four products (FdxA, PsmA and RedA) were expressed in the heterologous system. Ferredoxins, prismane-like proteins and NADH oxidoreductases are redox-active proteins and it is likely that the proteins on pTF5 represent an electron transport system of as yet unknown function. Surprisingly, although genes for redox-active proteins have been isolated from other bacteria by screening gene banks for increased sensitivity to metronidazole, the region of pTF5 containing the genes for these proteins was not responsible for the increase in metronidazole sensitivity conferred by the plasmid. The region of pTF5 which did confer increased metronidazole sensitivity to an E. coli metronidazole-resistant mutant was a 319 bp region of DNA close to the origin of plasmid replication. This region contained no ORFs and was identical to that previously reported for the replicon of a 9.8 kb T. ferrooxidans plasmid, pTF191.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
143 ( Pt 10)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3123-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9353917-Acidithiobacillus thiooxidans, pubmed-meshheading:9353917-Amino Acid Sequence, pubmed-meshheading:9353917-Anti-Bacterial Agents, pubmed-meshheading:9353917-Bacterial Proteins, pubmed-meshheading:9353917-Base Sequence, pubmed-meshheading:9353917-Chromosomes, Bacterial, pubmed-meshheading:9353917-Cloning, Molecular, pubmed-meshheading:9353917-DNA, Bacterial, pubmed-meshheading:9353917-Drug Resistance, Microbial, pubmed-meshheading:9353917-Electron Transport, pubmed-meshheading:9353917-Escherichia coli, pubmed-meshheading:9353917-Escherichia coli Proteins, pubmed-meshheading:9353917-Ferredoxins, pubmed-meshheading:9353917-Genes, Bacterial, pubmed-meshheading:9353917-Iron-Sulfur Proteins, pubmed-meshheading:9353917-Metronidazole, pubmed-meshheading:9353917-Molecular Sequence Data, pubmed-meshheading:9353917-Mutation, pubmed-meshheading:9353917-NADH, NADPH Oxidoreductases, pubmed-meshheading:9353917-Plasmids, pubmed-meshheading:9353917-Restriction Mapping, pubmed-meshheading:9353917-Sequence Homology, Amino Acid, pubmed-meshheading:9353917-Thiobacillus
pubmed:year
1997
pubmed:articleTitle
A geographically widespread plasmid from Thiobacillus ferrooxidans has genes for ferredoxin-, FNR-, prismane- and NADH-oxidoreductase-like proteins which are also located on the chromosome.
pubmed:affiliation
Department of Microbiology, University of Cape Town, South Africa.
pubmed:publicationType
Journal Article