Surface Acidic Amino Acid of Pseudomonas/Halomonas Chimeric Nucleoside Diphosphate Kinase Leads Effective Recovery from Heat- Denaturation

Author(s): Hiroko Tokunaga, Tsutomu Arakawa, Masao Tokunaga.

Journal Name: Protein & Peptide Letters

Volume 20 , Issue 7 , 2013

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One of the hallmarks of halophilic properties is reversibility of thermal unfolding. A nucleoside diphosphate kinase (NDK) from a moderate halophile Halomonas sp. 593 (HaNDK) follows this behavior. His-tagged chimeric NDK (HisPaHaNDK) consisting of an N-terminal half of a non-halophilic Pseuodomonas aeruginosa NDK (PaNDK) and a Cterminal half of HaNDK loses this reversible property, indicating a critical role of the N-terminal portion of PaNDK in determining the reversibility of the chimeric protein. Various mutations were introduced at Arg45 and Lys61, based on the model NDK structure. It appears that having Glu at position 45 is critical in conferring the thermal reversibility to HisPa- HaNDK chimeric protein.

Keywords: Acidic amino acid, halophilic, heat-denaturation, nucleoside diphosphate kinase, refolding, reversibility.

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Article Details

Year: 2013
Page: [836 - 841]
Pages: 6
DOI: 10.2174/0929866511320070015
Price: $58

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