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Soluble P-type ATPase from an archaeon, Methanococcus jannaschii
1Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, Japan.
FEBS Letters
|April 13, 2000
Summary
MJ0968, a protein lacking transmembrane domains, was investigated. It demonstrated ATPase activity, autophosphorylation, and vanadate inhibition, confirming it as a soluble P-type ATPase.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- MJ0968 shares high homology with the catalytic domain of P-type ATPases.
- MJ0968 lacks predicted transmembrane domains, questioning its P-type ATPase classification.
Purpose of the Study:
- To determine if MJ0968 functions as a P-type ATPase.
- To characterize the enzymatic activity of MJ0968.
Main Methods:
- Overexpression of MJ0968 in Escherichia coli.
- Purification of the recombinant MJ0968 protein.
- Assays for ATPase activity, autophosphorylation, and vanadate inhibition.
Main Results:
- Purified MJ0968 exhibited significant ATPase activity.
- The protein underwent autophosphorylation, a hallmark of P-type ATPases.
- Vanadate, a known inhibitor of P-type ATPases, effectively inhibited MJ0968 activity.
Conclusions:
- MJ0968 possesses biochemical properties consistent with a P-type ATPase.
- The findings identify MJ0968 as a soluble P-type ATPase, distinct from membrane-bound counterparts.
- This soluble form provides a new model for studying P-type ATPase mechanisms.