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A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins

Open access
Xu, Yao, Piston, David W., Johnson, Carl Hirschie·1999·Proceedings of the National Academy of Sciences

Abstract

We describe a method for assaying protein interactions that offers some attractive advantages over previous assays. This method, called bioluminescence resonance energy transfer (BRET), uses a bioluminescent luciferase that is genetically fused to one candidate protein, and a green fluorescent protein mutant fused to another protein of interest. Interactions between the two fusion proteins can bring the luciferase and green fluorescent protein close enough for resonance energy transfer to occur, thus changing the color of the bioluminescent emission. By using proteins encoded by circadian (daily) clock genes from cyanobacteria, we use the BRET technique to demonstrate that the clock protein KaiB interacts to form homodimers. BRET should be particularly useful for testing protein interactions within native cells, especially with integral membrane proteins or proteins targeted to specific organelles.

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Metadata

Authors
Xu, Y., Piston, D. W., & Johnson, C. H.
Venue
Proceedings of the National Academy of Sciences
Published
1999-01-05
Volume
96
Issue
1
Pages
151-156
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2126102214
Cited by
617
References
1
FWCI
7.94
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. https://app.cochat.ai/papers/10.1073/pnas.96.1.151
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Xu, Y., Piston, D. W., & Johnson, C. H. (1999). A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.1.151

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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