Secretional luciferase of the luminous shrimp Oplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase

FEBS Letters

Shimomura, Osamu¹  Inouye, Satoshi²  Nakamura, Hideshi³  Watanabe, Ken⁴ 

[1] Marine Biological Laboratory, Woods Hole, MA 02543, USA;Yokohama Research Center, Chisso Corporation, Kanazawa-ku, Yokohama 236-8605, Japan;Graduate School of Bioagricultural Science, Nagoya University, Nagoya 464-8601, Japan;National Institute for Longevity Sciences, Obu, Aichi 474-8522, Japan

关键词: Bioluminescence;    Luciferin;    Decapod;    Leucine-rich repeat sequence;    Reporter gene;    CMV;    cytomegalovirus;    HPLC;    high performance liquid chromatography;    PCR;    polymerase chain reaction;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(00)01963-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The deep-sea shrimp Oplophorus gracilirostris secretes a luciferase that catalyzes the oxidation of coelenterazine to emit blue light. The luciferase (M _r approx. 106 000) was found to be a complex composed of 35 kDa and 19 kDa proteins, and the cDNAs encoding these two proteins were cloned. The expression of the cDNAs in bacterial and mammalian cells indicated that the 19 kDa protein, not the 35 kDa protein, is capable of catalyzing the luminescent oxidation of coelenterazine. The primary sequence of the 35 kDa protein revealed a typical leucine-rich repeat sequence, whereas the catalytic 19 kDa protein shared no homology with any known luciferases including various imidazopyrazinone luciferases.

【 授权许可】

Unknown