Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum

被引：56
|
作者：
Pamnani, V
Tamura, T
Lupas, A
Peters, J
Cejka, Z
Ashraf, W
Baumeister, W
机构：
[1] MAX PLANCK INST BIOCHEM, D-82152 MARTINSRIED, GERMANY
[2] UNIV BRADFORD, DEPT BIOMED SCI, BRADFORD BD7 1DP, W YORKSHIRE, ENGLAND
来源：
FEBS LETTERS | 1997年 / 404卷 / 2-3期
关键词：
AAA family; ATPase; CDC48; p97; archaea; Thermoplasma acidophilum; PROTEIN SECONDARY STRUCTURE; PUTATIVE ATPASES; CELL-CYCLE; ESCHERICHIA-COLI; GENE-EXPRESSION; FAMILY; YEAST; PREDICTION; COMPLEX; MEMBER;
D O I：
10.1016/S0014-5793(97)00138-5
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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收藏
页码：263 / 268
页数：6
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