Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 Luciferases with Fluorescent (Antenna) Proteins: Bioluminescence Effects of the Aliphatic Additive

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• 作者：Valentin N. Petushkov ; Martijn Ketelaars ; Bruce G. Gibson ; and John Lee
• 刊名：Biochemistry
• 出版年：1996
• 出版时间：September 17, 1996
• 年：1996
• 卷：35
• 期：37
• 页码：12086 - 12093
• 全文大小：423K
• 年卷期：v.35,no.37(September 17, 1996)
• ISSN：1520-4995

文摘

The kinetics of the bacterial bioluminescence reaction is alteredin the presence of the fluorescent(antenna) proteins, lumazine protein (LumP) fromPhotobacterium or the yellow fluorescenceproteins(YFP) having FMN or Rf bound, from Vibrio fischeri strainY1. Depending on reaction conditions, thebioluminescence intensity and its decay rate may be either enhanced orstrongly quenched in the presenceof the fluorescent proteins. These effects can be simply explainedon the basis of the same protein-protein complex model that accounts for the bioluminescence spectralshifts induced by these fluorescentproteins. In such a complex, where the fluorophore evidently is inproximity to the luciferase active site,it is expected that the on-off rate of certain aliphatic componentsof the reaction should be altered witha consequent shift in the equilibria among the luciferaseintermediates, as recently elaborated in a kineticscheme. These aliphatic components are the bioluminescencereaction substrate, tetradecanal or otherlong-chain aldehyde, its carboxylic acid product, or dodecanol used asa stabilizer of the luciferaseperoxyflavin. No evidence can be found for the protein-proteininteraction in the absence of the aliphaticcomponent.