This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Downie, J A Articles by Gibson, F Search for Related Content PubMed PubMed Citation Articles by Downie, J A Articles by Gibson, F

Three genes coding for subunits of the membrane sector (F0) of the Escherichia coli adenosine triphosphatase complex.

ABSTRACT

Two mutant unc alleles, unc-469 and unc-476, have been characterized as affecting a previously undescribed gene, designated uncF. The uncF gene is part of the unc operon (with the gene order being uncBFEAGDC), although some uncertainty remains as to the relative order of the uncF and uncE genes. Mutant strains carrying the uncF469 or uncF476 allele lack the 18,000-molecular-weight component of the F0 sector of the adenosine triphosphatase in the cell membrane but retain the dicyclohexylcarbodiimide-binding protein (molecular weight, 8,400). Conversely, strains carrying mutations in the uncE gene lack the dicyclohexylcarbodiimide-binding protein but retain the 18,000-molecular-weight protein in the cell membrane. Strains carrying mutations in the uncB gene have both the 18,000-molecular-weight protein and the dicyclohexylcarbodiimide-binding protein present in the cell membranes. The three proteins of the F0 portion of the adenosine triphosphatase, viz., 24,000, 18,000, and 8,400 molecular weights, became membrane associated after in vitro transcription-translation with plasmid pAN51 as template. Plasmids carrying deletions which affected the UncBFE region were isolated from plasmid pAN51 and characterized genetically. A comparison of the genes that were absent from the various deletion plasmids with the membrane-associated products formed after in vitro transcription-translation indicated that the uncB gene coded for the 24,000-molecular-weight protein and that the gene order was probably uncBFE. A correlation between length of deoxyribonucleic acid, genes present, and their products is presented in relation to plasmid pAN51.

This article has been cited by other articles:

• Kol, S., Turrell, B. R., de Keyzer, J., van der Laan, M., Nouwen, N., Driessen, A. J. M. (2006). YidC-mediated Membrane Insertion of Assembly Mutants of Subunit c of the F1F0 ATPase. J. Biol. Chem. 281: 29762-29768 [Abstract] [Full Text]  
• Weber, J., Bowman, C., Senior, A. E. (1996). Specific Tryptophan Substitution in Catalytic Sites of Escherichia coli F1-ATPase Allows Differentiation between Bound Substrate ATP and Product ADP in Steady-state Catalysis. J. Biol. Chem. 271: 18711-18718 [Abstract] [Full Text]  
• Weber, J., Senior, A. E. (1995). Location and Properties of Pyrophosphate-binding Sites in Escherichia coli F[IMAGE]-ATPase. J. Biol. Chem. 270: 12653-12658 [Abstract] [Full Text]  
• Hermolin, J., Fillingame, R. H. (1995). Assembly of F(0) Sector of Escherichia coli H[IMAGE] ATP Synthase. J. Biol. Chem. 270: 2815-2817 [Abstract] [Full Text]