Reniformis

Fig. 4.6.1 Two examples of luminous anthozoans the sea pansy Renilla reniformis (left) and the sea pen Ptilosarcus gmneyi (right).

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. 

Charbonneau, H., and Cormier, M. J. (1979). Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein. J. Biol. Chem. 254 769-780. 

Cormier, M. J. (1961). Biochemistry of Renilla reniformis luminescence. In McElroy, W. D., and Glass, B. (eds.), Light and Life, pp. 274-293. Johns Hopkins Press, Baltimore. 

Cormier, M. J., and Dure, L. S. (1963). Studies on the bioluminescence of Balanoglossus biminiensis extracts. I. Requirement for hydrogen peroxide and characteristics of the system. J. Biol. Chem. 238 785-789. Cormier, M. J., and Hori, K. (1963). Studies on the bioluminescence of Renilla reniformis. IV. Non-enzymatic activation of Renilla luciferin. Biochim. Biophys. Acta 88 99-104. 

DeLuca, M., et al. (1971). Mechanism of oxidative carbon dioxide production during Renilla reniformis bioluminescence. Proc. Natl. Acad. Sci. USA 68 1658-1660. 

Hori, K., and Cormier, M. J. (1965). Studies on the bioluminescence of Renilla reniformis. V. Absorption and fluorescence characteristics of chromatographically pure luciferin. Biochim. Biophys. Acta 102 386-396. 

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. 

Kumar, S., et al. (1990). Amino acid sequence of the calcium-triggered luciferin binding protein of Renilla reniformis. FEBS Lett. 268 287-290. 

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. 

An examination of the flavonoids of Villarsia (Bohm et al., 1986) revealed a heterogeneous array of flavonol glycosides, based upon kaempferol, quercetin, and isorhamnetin, with each species exhibiting a unique assortment. Surprisingly, there were greater similarities between the pigment profile of V capensis and species from eastern Australia, V exaltata (Soland. ex Sims) G. Don from Tasmania and V. reniformis R. Br. from New South Wales, than with species native to... 

Messiano GB, da Silva T, Nascimento IR et al (2009) Biosynthesis of antimalarial lignans from Holostylis reniformis. Phytochemistry 70 590-596... 

Bact., Ins. (Sigma 2000) also marine Renilla reniformis (Pallas, 1766), Pennatulacea, Cnid. Cormiw 1994. 

Heinemann, S., Ehrlich, H., Douglas, T., Heinemann, C, Worch, H., Schatton, W., and Hanke, T. (2007). Ultrastructural studies on the collagen of the marine sponge Chondrosia reniformis Nardo. Biomacromolecules 8, 3452-3457. 

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