The subunit b of the F0F1-type ATPase of the bacterium Mycoplasma pneumoniae is a lipoprotein.
The DNA sequence analysis of the F0F1-ATPase operon of the bacterium Mycoplasma pneumoniae predicted that the subunit b, encoded by the gene atpF, is a lipoprotein of the murein lipoprotein type of Escherichia coli. Here we experimentally verify this prediction by metabolic labeling of subunit b with [14C]palmitic acid and by in vivo interfering with the processing of the prolipoprotein form of subunit b by the antibiotic globomycin, a specific inhibitor of the signal peptidase II. Our results suggest that the subunit b of the F0F1-ATPase of M. pneumoniae is anchored at the cytoplasmic membrane by an N-terminal lipid modification in addition to its transmembrane domain. The lipoprotein nature of subunit b and its proposed membrane topology seems to be characteristic for mycoplasmas, since among all sequenced bacterial atpF genes, only those from Mycoplasma gallisepticum and Mycoplasma genitalium code for a conserved lipoprotein consensus sequence.
Pyrowolakis
G
G
Zentrum für Molekulare Biologie Heidelberg, Mikrobiologie, Universität Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.
Hofmann
D
D
Herrmann
R
R
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D016384:Consensus Sequence; D004926:Escherichia coli / Q000201:enzymology; D008074:Lipoproteins / Q000737:chemistry* / Q000235:genetics*; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009177:Mycoplasma pneumoniae / Q000201:enzymology*; D019308:Palmitic Acid / Q000378:metabolism; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D008074:Lipoproteins; D046911:Macromolecular Substances; D019308:Palmitic Acid; D006180:Proton-Translocating ATPases