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

• Koshiba Takumi

  Department of Biology, Faculty of Sciences, Kyushu University

抄録

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.

収録刊行物

• Biophysics and Physicobiology

  Biophysics and Physicobiology 12 (0), 31-35, 2015

  一般社団法人 日本生物物理学会

キーワード

• antiviral innate immunity
• BRET
• mitochondria
• protein-protein interactions
• signal transduction

詳細情報

• CRID: 1390282680741415808
• NII論文ID: 130005098799
• DOI: 10.2142/biophysico.12.0_31
• ISSN: 21894779
• Web Site: https://www.jstage.jst.go.jp/article/biophysico/12/0/12_31/_pdf
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可