Pamnani V, Tamura T, Lupas A, Peters J, Cejka Z, Ashraf W, Baumeister W
Max-Planck-Institut für Biochemie, Martinsried, Germany.
FEBS Lett. 1997 Mar 10;404(2-3):263-8. doi: 10.1016/s0014-5793(97)00138-5.
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.
来自嗜热嗜酸栖热菌的Mg2(+)-ATP酶AAA家族的一个成员已被克隆并在大肠杆菌中表达。该蛋白，嗜热嗜酸栖热菌的VCP样ATP酶（VAT），是嗜酸硫化叶菌的SAV和盐生盐杆菌的CdcH的同源物，属于CDC48/VCP/p97亚家族。vat基因推导的产物长745个残基（Mr 83,000），在70℃时具有最佳的Mg2(+)-ATP酶活性。电子显微镜显示纯化的蛋白形成单环和双环同型六聚体环。尽管对称性不同，但由两个环形成的复合物的外观类似于20S蛋白酶体和Hsp60/GroEL。
