Efficient Expression of Haloarchaeal Nucleoside Diphosphate Kinase Via Strong Porin Promoter in Moderately Halophilic Bacteria

Author(s): Chizuru Nagayoshi, Hiroko Tokunaga, Aya Hayashi, Hiroaki Harazono, Kyoko Hamasaki, Ayumi Ando, Masao Tokunaga.

Journal Name: Protein & Peptide Letters

Volume 13 , Issue 6 , 2006

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Enzymes from extremely halophilic archaea require high concentration of salts for their proper folding and consequently are expressed as an unfolded and inactive form in Escherichia coli. Moderate halophile, which accumulates protein stabilizers, i.e., compatible solutes, is an attractive host cell for the recombinant production of heterologous proteins, since such protein stabilizers may help folding of expressed proteins. Here, we succeeded in efficient expression and purification to homogeneity of recombinant haloarchaeal nucleoside diphosphate kinase (HsNDK) in moderate halophile using newly isolated strong porin promoter.

Keywords: Halophilic, porin, protein expression, nucleoside diphosphate kinase, β-lactamase, reporter gene

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Article Details

Year: 2006
Page: [611 - 615]
Pages: 5
DOI: 10.2174/092986606777145760
Price: $58

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