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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Biophysical Society of Japan (BSJ)
2015
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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. |
format | Online Article Text |
id | pubmed-4736834 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT koshibatakumi proteinproteininteractionsofmitochondrialassociatedproteinviabioluminescenceresonanceenergytransfer |