Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-6-6
pubmed:databankReference
pubmed:abstractText
The arginine deiminase (ADI) pathway in Pseudomonas aeruginosa serves to generate ATP. The three enzymes involved, ADI, catabolic ornithine carbamoyltransferase and carbamate kinase, are induced by oxygen limitation and encoded by the contiguous arcABC genes. A 1.5-kb region upstream from arcABC was sequenced and found to contain an open reading frame, arcD, coding for a hydrophobic polypeptide of 52 kDa. The content and distribution of hydrophobic amino acids suggest that the arcD gene product may be a transmembrane protein. When arcD was fused to an Escherichia coli promoter, the ArcD protein was synthesized in E. coli maxicells and detected in the membrane fraction. In sodium dodecyl sulfate-polyacrylamide-gel electrophoresis the ArcD protein migrated like a 32-kDa protein; such anomalous electrophoretic mobility is known for other highly hydrophobic proteins. Mutations in arcD rendered the cells unable to utilize extracellular arginine as an energy source. Since anaerobic arginine consumption and ornithine release are coupled in P. aeruginosa, it is proposed that arcD specifies an arginine: ornithine antiporter or a part thereof. Insertions of IS21 or Tn1725 in arcD had a strong polar effect on the expression of the arcAB enzymes, indicating that the arc genes are organized as an arcDABC operon.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems, http://linkedlifedata.com/resource/pubmed/chemical/Antiporters, http://linkedlifedata.com/resource/pubmed/chemical/Arginine, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA Transposable Elements, http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Carbamoyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Carboxyl..., http://linkedlifedata.com/resource/pubmed/chemical/arginine deiminase, http://linkedlifedata.com/resource/pubmed/chemical/carbamate kinase
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-43
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:2158926-Amino Acid Sequence, pubmed-meshheading:2158926-Amino Acid Transport Systems, pubmed-meshheading:2158926-Anaerobiosis, pubmed-meshheading:2158926-Antiporters, pubmed-meshheading:2158926-Arginine, pubmed-meshheading:2158926-Bacterial Proteins, pubmed-meshheading:2158926-Base Sequence, pubmed-meshheading:2158926-Cloning, Molecular, pubmed-meshheading:2158926-DNA Transposable Elements, pubmed-meshheading:2158926-Escherichia coli, pubmed-meshheading:2158926-Genes, Bacterial, pubmed-meshheading:2158926-Genetic Complementation Test, pubmed-meshheading:2158926-Hydrolases, pubmed-meshheading:2158926-Membrane Proteins, pubmed-meshheading:2158926-Molecular Sequence Data, pubmed-meshheading:2158926-Mutation, pubmed-meshheading:2158926-Operon, pubmed-meshheading:2158926-Ornithine Carbamoyltransferase, pubmed-meshheading:2158926-Phosphotransferases, pubmed-meshheading:2158926-Phosphotransferases (Carboxyl Group Acceptor), pubmed-meshheading:2158926-Plasmids, pubmed-meshheading:2158926-Promoter Regions, Genetic, pubmed-meshheading:2158926-Protein Conformation, pubmed-meshheading:2158926-Pseudomonas aeruginosa
pubmed:year
1990
pubmed:articleTitle
The arc operon for anaerobic arginine catabolism in Pseudomonas aeruginosa contains an additional gene, arcD, encoding a membrane protein.
pubmed:affiliation
Mikrobiologisches Institut, Eidgenössische Technische Hochschule, Zürich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't