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来自极端嗜盐古菌盐沼盐杆菌的氯化钠激活的核苷二磷酸激酶在无盐条件下保持天然构象。

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

作者信息

Ishibashi M, Tokunaga H, Hiratsuka K, Yonezawa Y, Tsurumaru H, Arakawa T, Tokunaga M

机构信息

Laboratory of Applied Microbiology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.

出版信息

FEBS Lett. 2001 Mar 30;493(2-3):134-8. doi: 10.1016/s0014-5793(01)02292-x.

DOI:10.1016/s0014-5793(01)02292-x
PMID:11287010
Abstract

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.

摘要

来自极端嗜盐古菌的酶在没有高盐浓度的情况下很容易变性。然而,我们在此观察到,从盐生盐杆菌制备的核苷二磷酸激酶在无盐条件下具有活性且稳定,尽管它具有嗜盐酶的氨基酸组成特征。在大肠杆菌中表达的重组核苷二磷酸激酶在体外需要盐来激活,但一旦它获得正确的折叠,其活性和稳定性就不再需要盐的存在。

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