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Membrane-reversible H+-ATPase from Micrococcus lysodeikticus.
European Journal of Biochemistry
|March 1, 1976
Summary
Trypsin and dithiothreitol treatment enhance ATPase activity in Micrococcus lysodeikticus membrane fragments, enabling ATP to generate membrane potential. This suggests these agents affect a protein inhibitor of ATPase.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- Bacterial membrane fragments from Micrococcus lysodeikticus possess ATPase activity.
- Understanding the regulation of this ATPase activity is crucial for bacterial energy metabolism.
Purpose of the Study:
- To investigate the effect of trypsin and dithiothreitol on ATPase activity in M. lysodeikticus membrane fragments.
- To explore the relationship between ATPase activity and membrane potential generation.
Main Methods:
- Treatment of M. lysodeikticus membrane fragments with trypsin and dithiothreitol.
- Assay of ATPase activity.
- Measurement of transmembrane potential generation.
- Inhibition studies using dicyclohexylcarbodiimide.
Main Results:
- Trypsin and dithiothreitol treatment significantly increased ATPase activity in M. lysodeikticus membrane fragments.
- Treated membrane fragments gained the ability to convert ATP energy into a transmembrane potential difference.
- Dicyclohexylcarbodiimide inhibited both ATPase activity and the coupled generation of membrane potential.
- The observed increase in ATPase activity is hypothesized to be due to the agents' effect on a protein inhibitor of ATPase.
Conclusions:
- Trypsin and dithiothreitol activate ATPase in M. lysodeikticus membranes, likely by modulating a protein inhibitor.
- This activation facilitates the conversion of ATP hydrolysis into membrane potential, highlighting a regulatory mechanism in bacterial energy transduction.