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Journal Article

Cloning, sequencing and expression of vat, a cdc48/p97 atpase homologue from the archaeon thermoplasma acidophilum

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Pamnani, V., Tamura, T., Lupas, A., Peters, J., Cejka, Z., Ashraf, W., et al. (1997). Cloning, sequencing and expression of vat, a cdc48/p97 atpase homologue from the archaeon thermoplasma acidophilum. FEBS Letters, 404(2-3), 263-268.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-729E-9
Abstract
A member of the AAA family of Mg2+-ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli. The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocaldarius and CdcH of Halobacterium salinarium, and belongs to the CDC48/VCP/p97 subfamily. The deduced product of the vat gene is 745 residues long (M(r) 83 000), which has an optimal Mg2+-ATPase activity at 70 degrees C. Electron microscopy shows the purified protein to form single and double homo-hexameric rings, Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL. (C) 1997 Federation of European Biochemical Societies. [References: 42]