OppA, the Substrate-Binding Subunit of the Oligopeptide Permease, Is the Major Ecto-ATPase ofMycoplasma hominis

Autor: Miriam Hopfe, Birgit Henrich
Rok vydání: 2004
Předmět:
Zdroj: Journal of Bacteriology. 186:1021-1028
ISSN: 1098-5530
0021-9193
DOI: 10.1128/jb.186.4.1021-1028.2004
Popis: Most ATPases, involved in energy-driven processes, act in the cytoplasm. However, external membrane-bound ATPases have also been described in parasites and eukaryotic cells. InMycoplasma hominis, a bacterium lacking a cell wall, the surface-exposed substrate-binding protein OppA of an oligopeptide permease (Opp) contains an ATP binding P-loop structure in the C-terminal region. With ATP affinity chromatography and tryptic digestion in the presence or absence of ATP, the functionality of the Mg2+-dependent ATP binding site is demonstrated. In addition to ATP, ADP also could bind to OppA. The presence of an ATPase activity on the surface ofM. hominisis indicated by the inactivation of ATP hydrolyzing activity of intact mycoplasma cells by the impermeable ATPase inhibitor 4′,4′-diisothiocyanostilbene-2′,2′-disulfonic acid and influenced by the ATP analog 5′-fluorosulfonyl-benzoyladenosine. Comparing equimolar amounts of OppA in intact mycoplasma cells and in the purified form indicated that more than 80% of the surface-localized ATPase activity is derived from OppA, implying that OppA is the main ATPase on the surface of mycoplasma cells. Together, these data present the first evidence that the cytoadhesive substrate binding protein OppA of the oligopeptide permease also functions as an ecto-ATPase inMycoplasma hominis.
Databáze: OpenAIRE