Purification and molecular cloning of the group II chaperonin from the acidothermophilic archaeon, Sulfolobus sp. strain 7.
To elucidate the structure and functional mechanism of the group II chaperonin, molecular cloning of the gene for and purification of the group II chaperonin from the thermoacidophilic archaeon Sulfolobus sp. strain 7 were performed. The purified Sulfolobus chaperonin exhibited weak ATPase activity and arrested the spontaneous refolding of the thermophilic lactate dehydrogenase. However, the refolding could not be resumed by addition of ATP. The chaperonin consists of two kinds of subunits, alpha and beta, the deduced amino acid sequences of which were highly homologous to those of TF56 and TF55 from Sulfolobus shibatae, respectively.
Nakamura
N
N
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Taguchi
H
H
Ishii
N
N
Yoshida
M
M
Suzuki
M
M
Endo
I
I
Miura
K
K
Yohda
M
M
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000595:Amino Acid Sequence; D019843:Archaeal Proteins; D001483:Base Sequence; D018833:Chaperonins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry; D056385:Group II Chaperonins; D007770:L-Lactate Dehydrogenase / Q000737:chemistry; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017510:Protein Folding; D017422:Sequence Analysis, DNA; D017385:Sequence Homology; D016944:Sulfolobus / Q000737:chemistry*
D019843:Archaeal Proteins; D004269:DNA, Bacterial; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase; D018833:Chaperonins; D056385:Group II Chaperonins