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 (Mr 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.
MeSH terms
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Adenosine Triphosphatases / biosynthesis*
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / ultrastructure
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Amino Acid Sequence
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Archaeal Proteins
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Ca(2+) Mg(2+)-ATPase / biosynthesis*
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Ca(2+) Mg(2+)-ATPase / chemistry
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Ca(2+) Mg(2+)-ATPase / ultrastructure
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Cell Cycle Proteins / chemistry
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Cloning, Molecular
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Escherichia coli
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Genes, Bacterial
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Halobacterium / enzymology
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Microscopy, Electron
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Molecular Sequence Data
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Molecular Weight
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / ultrastructure
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Sequence Homology, Amino Acid
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Sulfolobus / enzymology
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Thermoplasma / enzymology*
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Thermoplasma / genetics
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Valosin Containing Protein
Substances
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Archaeal Proteins
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Cell Cycle Proteins
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Recombinant Proteins
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Adenosine Triphosphatases
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Ca(2+) Mg(2+)-ATPase
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Valosin Containing Protein
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vat protein, Thermoplasma acidophilum