Contribution of Halophilic Nucleoside Diphosphate Kinase Sequence to the Heat Stability of Chimeric Molecule

Title: Contribution of Halophilic Nucleoside Diphosphate Kinase Sequence to the Heat Stability of Chimeric Molecule

Volume: 13 Issue: 5

Author(s): Hiroko Tokunaga, Yuuki Oda, Yasushi Yonezawa, Tsutomu Arakawa and Masao Tokunaga

Affiliation:

Keywords: Halophilic, Nucleoside Diphosphate Kinase, Halomonas, Pseudomonas aeruginosa, Chimera, Heat Stability, Refolding

Abstract: A halophilic nucleoside diphosphate kinase from a moderate halophile, Halomonas sp. 593 (593NDK), was found to be resistant to heat treatment, as indicated by the high level of activity recovery after heating at high temperatures. This is due to reversibility of thermal unfolding, not the high melting temperature, of the protein. The highly homologous NDK from non-halophilic organism, Pseudomonas aeruginosa, showed instability against heat treatment. Chimeric molecules consisting of each half of these two NDKs were constructed and characterized for their heat stability. The results showed that the N-terminal half of 593NDK contributes to the heat stability of the proteins. We discuss the possible reason for the observed difference in resistance to heat treatment between the 593NDK and PaNDK and between two chimeric proteins.

Cite this article as:

Tokunaga Hiroko, Oda Yuuki, Yonezawa Yasushi, Arakawa Tsutomu and Tokunaga Masao, Contribution of Halophilic Nucleoside Diphosphate Kinase Sequence to the Heat Stability of Chimeric Molecule, Protein & Peptide Letters 2006; 13 (5) . https://dx.doi.org/10.2174/092986606776819628

DOI https://dx.doi.org/10.2174/092986606776819628	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305