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Immunochemical evidence for an active (F1-F0)-ATPase in mycoplasmas
S Rottem1, M H Shirvan, M F Barile
1Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Abstract:
In all Acholeplasma, Mycoplasma and Spiroplasma species tested, a protein capable of reacting with antibodies prepared against the beta subunit of the proton-ATPase complex from yeast, chloroplasts and Escherichia coli was detected. The reactive protein of M. gallisepticum was found to be catalytically active, suggesting that mycoplasmas, as other bacteria, possess a proton-translocating ATPase. Characterization of the ATPase activity of M. gallisepticum indicates that this organism also possesses a Na+-stimulated ATPase activity that differs from the proton-ATPase in its pH profile and its resistance to dicyclohexylcarbodiimide (DCCD).
Insights
Mycoplasmas possess a proton-translocating ATPase, similar to other bacteria. This study identified a catalytically active proton-ATPase in Mycoplasma gallisepticum, also revealing a distinct Na+-stimulated ATPase activity.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Mycoplasmas are bacteria lacking a cell wall.
- The proton-translocating ATPase (proton-ATPase) is crucial for energy metabolism in many organisms.
- Previous studies have not definitively identified proton-ATPases in all mycoplasma species.
Purpose of the Study:
- To investigate the presence and activity of proton-ATPases in various mollicute species (Acholeplasma, Mycoplasma, Spiroplasma).
- To characterize the ATPase activity in Mycoplasma gallisepticum.
Main Methods:
- Immunological detection using antibodies against the beta subunit of proton-ATPase from yeast, chloroplasts, and E. coli.
- Enzyme activity assays to measure ATPase function in M. gallisepticum.
- Characterization of ATPase activity including pH profile and inhibitor resistance (DCCD).
Main Results:
- A protein reactive to proton-ATPase antibodies was detected in all tested Acholeplasma, Mycoplasma, and Spiroplasma species.
- The reactive protein in M. gallisepticum exhibited catalytic activity, indicating a functional proton-ATPase.
- M. gallisepticum also displayed a unique Na+-stimulated ATPase activity, distinct from the proton-ATPase.
Conclusions:
- Mycoplasmas, like other bacteria, possess a proton-translocating ATPase.
- Mycoplasma gallisepticum has both a proton-ATPase and a separate Na+-stimulated ATPase.
- These findings contribute to understanding energy metabolism in mycoplasmas.