Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum.
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.
Pamnani
V
V
Max-Planck-Institut für Biochemie, Martinsried, Germany. pamnani@vms.biochem.mpg.de
Tamura
T
T
Lupas
A
A
Peters
J
J
Cejka
Z
Z
Ashraf
W
W
Baumeister
W
W
D000251:Adenosine Triphosphatases / Q000096:biosynthesis* / Q000737:chemistry / Q000648:ultrastructure; D000595:Amino Acid Sequence; D019843:Archaeal Proteins; D017301:Ca(2+) Mg(2+)-ATPase / Q000096:biosynthesis* / Q000737:chemistry / Q000648:ultrastructure; D018797:Cell Cycle Proteins / Q000737:chemistry; D003001:Cloning, Molecular; D004926:Escherichia coli; D005798:Genes, Bacterial; D006217:Halobacterium / Q000201:enzymology; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid; D016944:Sulfolobus / Q000201:enzymology; D013822:Thermoplasma / Q000201:enzymology* / Q000235:genetics; D000074405:Valosin Containing Protein
D019843:Archaeal Proteins; D018797:Cell Cycle Proteins; D011994:Recombinant Proteins; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000074405:Valosin Containing Protein; C105134:vat protein, Thermoplasma acidophilum