Luciferase Gaussia

Verhaegen, M., and Christopoulos, T. K. (2002). Recombinant Gaussia luciferase. Overexpression, purification, and analytical application of a bioluminescent reporter for DNA hybridization. Anal. Chem. 74 4378-4385. 

Gaussia luciferase G-Luc Gaussia princeps Shao and Bock [51] Codon-optimized luciferase... 

M. (2008) Gaussia-luciferase as a sensitive reporter gene for monitoring promoter activity in the nucleus of the green alga Chlamydomonas reinhardtii. Mol. Genet. Genomics, 280 (2), 153-162. 

Luker, K., Mihalko, L., Schmidt, B., Lewin, S., Ray, P., Shcherbo, D., etal. (2012). In vivo imaging of lig3nd receptor binding tvith Gaussia luciferase complementation. Nature Medicine, 18, 172-177. 

Remy, I., Michnick, S. (2006). A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nature Methods, 3, 977—979. 

In a reporter gene assay, CKR-mediated activation of transcription factors can be quantified. A plasmid encoding the CKR of interest is cotransfected with a plasmid encoding a reporter protein of which expression can easily be detected, such as firefly luciferase (Flue) (or another bioluminescent protein or enzyme such as Gaussia luciferase (Glue) or P-galactosidase). Luciferase transcription is controUed by an inducible promoter containing multiple response elements for a specific transcription factor. Hence, activation (or inhibition) of this transcription factor in response to CKR activation leads to the expression of luciferase (Fig. 15A). 

Chung, E., et al. Secreted Gaussia luciferase as a biomarker for monitoring tumor progression and treatment response of systemic metastases. PloS One 4(12), e8316... 

Suzuki, X. Usuda, S. Ichinose, H. Inouye, S. Realtime bioluminescence imaging of a protein secretory pathway in living mammalian cells using Gaussia luciferase. FEBS Lett. 2007, 581, 4551 556. 

Coelenterazine can be detected and measured with a coelenterazine luciferase, i.e. a luciferase specific to coelenterazine. As the coelenterazine luciferase, the luciferases from the sea pansy Renilla and the copepods Gaussia and Pleuromamma are commercially available. Certain kinds of decapod shrimps, such as Oplophoms and Heterocarpus, contain a large amount of luciferase, and the luciferases purified from them are most satisfactory for the assay of coelenterazine considering their high activities and high quantum yields. Even partially purified preparations of these luciferases are satisfactory for most measurements. The author routinely uses purified Oplophoms luciferase. 

Ballou, B., Szent-Gyorgyi, C., and Finley, G. (2000). Properties of a new luciferase from the copepod Gaussia princeps. 11th Int. Symp. on Biolumin. Chemilumin., Abstract p. 34. Asilomar, CA. 

Shao, N. and Bock, R. (2008) A codon-optimized luciferase from Gaussia princeps facilitates the in vivo monitoring of gene expression in the model alga Chlamydomonas reinhardtii. Cum Genet., 53 (6), 381-388. 

An important note regarding the selection of luciferase reporters in chemical screens is the susceptibility of FL to chemical inhibition that could give rise to false positives [11]. In our experience, enzymes such as Renilla, Gaussia, or Nanoluc luciferase (RX, GL, and NL, respectively) that utilize coelen-terazine (a larger substrate than luciferin) are less susceptible to chemical inhibition. Thus, given the opportunity to select or design a reporter construct with a chemical screen in mind, avoidance of FL would be advised. 

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