Linked Life Data

7623667

Source:http://linkedlifedata.com/resource/pubmed/id/7623667

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-8-31
pubmed:databankReference
pubmed:abstractText
A mutant of Escherichia coli K-12, JCB606, which lacks all five c-type cytochromes synthesized during anaerobic growth in the presence of nitrite or trimethylamine-N-oxide (TMAO), was totally defective in Nrf activity and also partially defective in TMAO reductase activity. The mutation in strain JCB606 was shown to affect expression of the tor operon, which contributes almost equally with the products of the dms operon to the rate of TMAO reduction by bacteria during anaerobic growth in the presence of TMAO. The mutation in strain JCB606, dipZ, was mapped by P1 transduction close to the mel operon at co-ordinate 4425 on the E. coli chromosome, the gene order being nrf-fdhF-mel-dipZ-ampC. Recombinant plasmids that restored Nrf activity to test-tube cultures of the mutant were isolated from a cosmid library. A 2.7 kb EcoRV-SmaI fragment (co-ordinates 4443 to 4446 kb on the physical map of the E. coli chromosome) was found potentially to encode three genes arranged in at least two operons. The second gene, dipZ, was sufficient to complement the JCB606 mutation. The translated DNA sequence predicts that DipZ is a 53 kDa integral membrane protein with a 37 kDa N-terminal domain including at least six membrane-spanning helices and a 16 kDa carboxy-terminal hydrophilic domain which includes a protein disulphide isomerase-like motif. It is suggested that DipZ is essential for maintaining cytochrome c apoproteins in the correct conformations for the covalent attachment of haem groups to the appropriate pairs of cysteine residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:geneSymbol
dipZ
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1139-50
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7623667-Amino Acid Sequence, pubmed-meshheading:7623667-Base Sequence, pubmed-meshheading:7623667-Cloning, Molecular, pubmed-meshheading:7623667-Cytochrome c Group, pubmed-meshheading:7623667-Escherichia coli, pubmed-meshheading:7623667-Escherichia coli Proteins, pubmed-meshheading:7623667-Formates, pubmed-meshheading:7623667-Genes, Bacterial, pubmed-meshheading:7623667-Genetic Complementation Test, pubmed-meshheading:7623667-Isomerases, pubmed-meshheading:7623667-Membrane Proteins, pubmed-meshheading:7623667-Methylamines, pubmed-meshheading:7623667-Molecular Sequence Data, pubmed-meshheading:7623667-Mutation, pubmed-meshheading:7623667-Nitrites, pubmed-meshheading:7623667-Open Reading Frames, pubmed-meshheading:7623667-Operon, pubmed-meshheading:7623667-Oxidation-Reduction, pubmed-meshheading:7623667-Oxidoreductases, pubmed-meshheading:7623667-Promoter Regions, Genetic, pubmed-meshheading:7623667-Protein Disulfide-Isomerases, pubmed-meshheading:7623667-Recombinant Fusion Proteins, pubmed-meshheading:7623667-Restriction Mapping, pubmed-meshheading:7623667-Sequence Analysis, DNA, pubmed-meshheading:7623667-Transcription, Genetic
pubmed:year
1995
pubmed:articleTitle
The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain.
pubmed:affiliation
School of Biochemistry, University of Birmingham, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't