Expression of subunits a and c of the sodium-dependent ATPase of Propionigenium modestum in Escherichia coli

The aim of the present study was to construct functional hybrid ATPases consisting of all Escherichia coli ATPase subunits excepts the F0 subunits a or c which were replaced by the respective subunits of the Propionigenium modestum ATPase. This would give valuable information on the subunit(s) confe...

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Bibliographic Details
Published in:Archives of microbiology 1994, Vol.161 (6), p.495-500
Main Authors: GERIKE, U, DIMROTH, P
Format: Article
Language:English
Subjects:
Bacterial Proteins - biosynthesis
Bacterial Proteins - genetics
Bacterial Proton-Translocating ATPases
Bacteriology
Base Sequence
Biological and medical sciences
Escherichia coli
Escherichia coli - drug effects
Escherichia coli - genetics
Escherichia coli - growth & development
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Bacterial
Genes, Bacterial - genetics
Genetic Complementation Test
Genetics
Gram-Negative Anaerobic Bacteria - enzymology
Gram-Negative Anaerobic Bacteria - genetics
Microbiology
Molecular Sequence Data
Operon
Propionigenium modestum
Proton-Translocating ATPases - biosynthesis
Proton-Translocating ATPases - chemistry
Proton-Translocating ATPases - genetics
Protons
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - genetics
Sodium - pharmacology
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Summary:The aim of the present study was to construct functional hybrid ATPases consisting of all Escherichia coli ATPase subunits excepts the F0 subunits a or c which were replaced by the respective subunits of the Propionigenium modestum ATPase. This would give valuable information on the subunit(s) conferring the coupling ion specificity. Plasmids were constructed that carried the gene for subunit c (uncE) or subunit a (uncB) behind a tac promoter. These plasmids were transformed into E. coli strains which differed with respect to the unc operon and the expression of the P. modestum genes was verified biochemically. Enhanced expression of the P. modestum genes led to strong growth inhibition of all E. coli strains tested. However, the expressed P. modestum proteins could not functionally complement E. coli strains that lacked the homologous subunit.
ISSN:0302-8933
1432-072X
DOI:10.1007/BF00307770