OppA, the Substrate-Binding Subunit of the Oligopeptide Permease, Is the Major Ecto-ATPase ofMycoplasma hominis
Autor: | Miriam Hopfe, Birgit Henrich |
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Rok vydání: | 2004 |
Předmět: |
Adenosine Triphosphatases
Oligopeptide biology Permease Lipoproteins Protein subunit ATPase Binding protein Mycoplasma hominis biology.organism_classification Enzymes and Proteins Microbiology Molecular biology Protein Subunits chemistry.chemical_compound Adenosine Triphosphate Bacterial Proteins Biochemistry chemistry biology.protein Binding site Carrier Proteins Molecular Biology Adenosine triphosphate |
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 |
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