Renilla reniformis luciferase

Karkhanis, Y. D., and Cormier, M. J. (1971). Isolation and properties of Renilla reniformis luciferase, a low molecular weight energy conversion enzyme. Biochemistry 10 317-326. 

Liu, J., O Kane, D. J., and Escher, A. (1997). Secretion of functional Renilla reniformis luciferase by mammalian cells. Gene 203 141-148. 

Lorenz, W. W., et al. (1996). Expression of the Renilla reniformis luciferase gene in mammalian cells./. Biolumin. Chemilumin. 11 31-37. 

BRET is based on the non-radiative transfer of energy between a biolumi-nescent donor protein (e.g. firefly or Renilla reniformis luciferase) and a... 

Matthews JC, Hori K, Cormier MJ. Purification and properties of Renilla reniformis luciferase. Biochemistry 1977 16 85-91. 

Srikantha T, Klapach A, Lorenz WW, Tsai LK, LaughUn LA, Gorman JA, Soil DR. The sea pansy Renilla reniformis luciferase serves as a sensitive bioluminescent reporter for differential gene expression in Candida albicans. J Bacteriol 1996 178 121-129. 

Renilla luciferase. The luciferase of Renilla reniformis has been purified and characterized by Karkhanis and Cormier (1971) and Matthews et al. (1977a). The purified luciferase has a molecular weight of 35,000, and catalyzes the luminescence reaction of coelenterazine. The luciferase-catalyzed luminescence is optimum at pH 7.4, at a temperature of 32°C, and in the presence of 0.5 M salt (such as NaCl or KC1). The luciferase has a specific activity of 1.8 x 1015 photons s"1mg"1, and a turnover number of 111/min. The luminescence spectrum shows a maximum at 480 nm. The absorbance A28O of a 0.1% luciferase solution is 2.1. The luciferase has a tendency to self-aggregate, forming higher molecular weight species of lower luminescence activities. 

The cDNA encoding the luciferase of Renilla reniformis has been obtained and expressed in Escherichia coli (Lorenz et al., 1991). The cDNA contained an open reading frame encoding a 314-amino acid sequence. The recombinant Renilla luciferase obtained had a molecular weight of 34,000, and showed an emission maximum at 480 nm in the luminescence reaction of coelenterazine, in good agreement with the data of natural Renilla luciferase. 

Hart, R. C., Matthews, J. C., Hori, K., and Cormier, M. J. (1979). Renilla reniformis bioluminescence Luciferase-catalyzed production of nonradiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein. Biochemistry 18 2204-2210. 

Kreiss, P., and Cormier, M. J. (1967). Inhibition of Renilla reniformis bioluminescence by light effects on luciferase and its substrates. Biochim. Biophys. Acta 141 181-183. 

The sea pansy, Renilla reniformis, contains a luciferase K luciferin = 30 nmol 1 pH optimum... 

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