Document Detail

Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase.
MedLine Citation:
PMID:  21839770     Owner:  NLM     Status:  Publisher    
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.
Matsujiro Ishibashi; Keiko Ida; Shuhei Tatsuda; Tsutomu Arakawa; Masao Tokunaga
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-8-5
Journal Detail:
Title:  International journal of biological macromolecules     Volume:  -     ISSN:  1879-0003     ISO Abbreviation:  -     Publication Date:  2011 Aug 
Date Detail:
Created Date:  2011-8-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7909578     Medline TA:  Int J Biol Macromol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011 Elsevier B.V. All rights reserved.
Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890 0065, Japan.
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