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Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer

Protein-protein interactions are essential biological reactions occurring at inter- and intra-cellular levels. The analysis of their mechanism is generally required in order link to understand their various cellular functions. Bioluminescence resonance energy transfer (BRET), which is based on an en...

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Autor principal: Koshiba, Takumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736834/
https://www.ncbi.nlm.nih.gov/pubmed/27493852
http://dx.doi.org/10.2142/biophysico.12.0_31
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author Koshiba, Takumi
author_facet Koshiba, Takumi
author_sort Koshiba, Takumi
collection PubMed
description Protein-protein interactions are essential biological reactions occurring at inter- and intra-cellular levels. The analysis of their mechanism is generally required in order link to understand their various cellular functions. Bioluminescence resonance energy transfer (BRET), which is based on an enzymatic activity of luciferase, is a useful tool for investigating protein-protein interactions in live cells. The combination of the BRET system and biomolecular fluorescence complementation (BiFC) would provide us a better understanding of the hetero-oligomeric structural states of protein complexes. In this review, we discuss the application of BRET to the protein-protein interactions of mitochondrial-associated proteins and discuss its physiological relevance.
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spelling pubmed-47368342016-08-04 Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer Koshiba, Takumi Biophys Physicobiol Review Article Protein-protein interactions are essential biological reactions occurring at inter- and intra-cellular levels. The analysis of their mechanism is generally required in order link to understand their various cellular functions. Bioluminescence resonance energy transfer (BRET), which is based on an enzymatic activity of luciferase, is a useful tool for investigating protein-protein interactions in live cells. The combination of the BRET system and biomolecular fluorescence complementation (BiFC) would provide us a better understanding of the hetero-oligomeric structural states of protein complexes. In this review, we discuss the application of BRET to the protein-protein interactions of mitochondrial-associated proteins and discuss its physiological relevance. The Biophysical Society of Japan (BSJ) 2015-09-09 /pmc/articles/PMC4736834/ /pubmed/27493852 http://dx.doi.org/10.2142/biophysico.12.0_31 Text en 2015 © The Biophysical Society of Japan This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Koshiba, Takumi
Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
title Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
title_full Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
title_fullStr Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
title_full_unstemmed Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
title_short Protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
title_sort protein-protein interactions of mitochondrial-associated protein via bioluminescence resonance energy transfer
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736834/
https://www.ncbi.nlm.nih.gov/pubmed/27493852
http://dx.doi.org/10.2142/biophysico.12.0_31
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