NaCl‐activated nucleoside diphosphate kinase from extremely halophilic archaeon, Halobacterium salinarum, maintains native conformation without salt

FEBS Letters

Hiratsuka, Kazushi¹  Arakawa, Tsutomu²  Tsurumaru, Hirohito¹  Yonezawa, Yasushi¹  Tokunaga, Hiroko¹  Ishibashi, Matsujiro¹  Tokunaga, Masao¹ 

[1] Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan;Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA

关键词: Halophilic;    Salt;    Nucleoside diphosphate kinase;    Cloning;    ndk;    Halobacterium;    NDK;    nucleoside diphosphate kinase;    HsNDK;    NDK from Halobacterium salinarum;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(01)02292-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Enzymes from extremely halophilic archaea are readily denatured in the absence of a high salt concentration. However, we have observed here that a nucleoside diphosphate kinase prepared from Halobacterium salinarum was active and stable in the absence of salt, though it has the amino acid composition characteristic of halophilic enzymes. Recombinant nucleoside diphosphate kinase expressed in Escherichia coli requires salt for activation in vitro, but once it acquires the proper folding, it no longer requires the presence of salts for its activity and stability.

【 授权许可】

Unknown