NDLI: Bioluminescence Resonance Energy Transfer (BRET) Allows Monitoring the Barnase-Barstar Complex In Vivo

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Bioluminescence Resonance Energy Transfer (BRET) Allows Monitoring the Barnase-Barstar Complex In Vivo

Content Provider	MDPI
Author	Marchenkov, Victor Ivashina, Tanya Marchenko, Natalia Ksenzenko, Vladimir Semisotnov, Gennady
Copyright Year	2022
Description	Bioluminescence resonance energy transfer (BRET) seems to be a promising biophysical technique to study protein–protein interactions within living cells due to a very specific reaction of bioluminescence that essentially decreases the background of other cellular components and light-induced destruction of biomacromolecules. An important direction of the development of this technique is the study of known strong protein–protein complexes in vivo and the estimation of an average distance between chromophores of the donor and acceptor. Here, we demonstrate an in vivo interaction between barnase fused with luciferase (from Renilla reniformis, RLuc) and barstar fused with EGFP (enhanced green fluorescent protein of Aequorea victoria) monitored by BRET. The distance between the luciferase and EGFP chromophores within the complex has been evaluated as equal to (56 ± 2) Å.
Ending Page	78
Page Count	7
Starting Page	72
e-ISSN	26734125
DOI	10.3390/biophysica2010007
Journal	Biophysica
Issue Number	1
Volume Number	2
Language	English
Publisher	MDPI
Publisher Date	2022-02-07
Access Restriction	Open
Subject Keyword	Biophysica Protein–protein Interactions Fusion Proteins Photoproteins Bret Barnase Barstar
Content Type	Text
Resource Type	Article

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