Purification and molecular cloning of the group II chaperonin from the acidothermophilic archaeon, Sulfolobus sp. strain 7

N Nakamura; H Taguchi; N Ishii; M Yoshida; M Suzuki; I Endo; K Miura; M Yohda

doi:10.1006/bbrc.1997.6916

Purification and molecular cloning of the group II chaperonin from the acidothermophilic archaeon, Sulfolobus sp. strain 7

Biochem Biophys Res Commun. 1997 Jul 30;236(3):727-32. doi: 10.1006/bbrc.1997.6916.

Authors

N Nakamura¹, H Taguchi, N Ishii, M Yoshida, M Suzuki, I Endo, K Miura, M Yohda

Affiliation

¹ Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.

PMID: 9245723
DOI: 10.1006/bbrc.1997.6916

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Triphosphate / pharmacology
Amino Acid Sequence
Archaeal Proteins
Base Sequence
Chaperonins / chemistry
Chaperonins / genetics*
Chaperonins / metabolism
DNA, Bacterial / chemistry
Group II Chaperonins
L-Lactate Dehydrogenase / chemistry
Microscopy, Electron
Molecular Sequence Data
Polymerase Chain Reaction
Protein Folding
Sequence Analysis, DNA
Sequence Homology
Sulfolobus / chemistry*

Substances

Archaeal Proteins
DNA, Bacterial
Adenosine Triphosphate
L-Lactate Dehydrogenase
Chaperonins
Group II Chaperonins

Associated data

GENBANK/AB001085
GENBANK/AB001086