Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression |
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Authors: | Tang Wai-Kwan Chan Chi-Bun Cheng Christopher H K Fong Wing-Ping |
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Institution: | Department of Biochemistry, The Chinese University of Hong Kong, Shatin, NT, Hong Kong, China. |
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Abstract: | Subsequent to our earlier report on the first purification of antiquitin protein from seabream liver and demonstration of its enzymatic activity FEBS Letters 516 (2002) 183-186], we report herein the cloning of its full-length cDNA sequence. The open reading frame encodes a protein of 511 amino acids. Results of RT-PCR indicate that antiquitin is highly expressed in both the seabream liver and kidney. Transfection studies in cultured eukaryotic cells provided further evidence that it is a cytosolic protein. Bacterial expression of the enzyme was also performed. The purified recombinant protein was demonstrated to exhibit similar kinetic properties as the native enzyme. |
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