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Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase.

Abstract：

:We have previously reported that amino-terminal extension sequence containing hexa-His facilitated refolding and assembly of hexameric nucleoside diphosphate kinase from extremely halophilic archaeon Halobacterium salinarum (NDK). In this study, we made various mutations in both the tag sequence and within NDK molecule. SerNDK, in which hexa-His was replaced with hexa-Ser, showed no facilitated folding. In addition, HisD58GD63G, in which both Asp58 and Asp63 in NDK were replaced with Gly, also showed no refolding enhancement. These results suggest that hexa-His in His-tag interact cooperatively with either Asp58 or Asp63 or both. Furthermore, G114D mutant, which formed a dimer in low salt solution, was strongly stabilized by His-tag to form a stable hexamer.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Ishibashi M,Ida K,Tatsuda S,Arakawa T,Tokunaga M

doi

10.1016/j.ijbiomac.2011.07.014

subject

Has Abstract

pub_date

2011-11-01 00:00:00

pages

778-83

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(11)00292-3

journal_volume

49

pub_type

杂志文章

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