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

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.

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Pamnani, V., Author
Tamura, T., Author
Lupas, A.1, Author              
Peters, J.1, Author              
Cejka, Z., Author
Ashraf, W., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Aaa family; Atpase; Cdc48; p97; Archaea; Thermoplasma acidophilum.; Protein secondary structure; Putative atpases; Cell-cycle; Escherichia-coli; Gene-expression; Family; Yeast; Prediction; Complex; Member.; Biochemistry & biophysics.
 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]

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 Dates: 1997-03-10
 Publication Status: Published in print
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 Identifiers: eDoc: 318521
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 404 (2-3) Sequence Number: - Start / End Page: 263 - 268 Identifier: -