Protein–Protein Interaction Analysis Using Proximity Biotinylation Enzymes

• Sawasaki Tatsuya

  Proteo-Science Center (PROS), Ehime University

Bibliographic Information

Other Title

• 近位依存性ビオチン化酵素によるタンパク質相互作用解析

Abstract

Many proteins in the organisms function by interacting with other proteins to form complexes. Especially in higher organisms such as human, the formation of complex protein is one of the mechanisms that regulate protein function. Therefore, the analysis of interacting proteins is an important issue to understand the complicated regulatory mechanisms that sustain the higher organisms. As a method to analyze interacting proteins, the BioID technique has been developed in which a proximity biotinylation enzyme is fused to the target protein for labeling the proximal proteins with biotin. Recently, we have succeeded in developing a novel proximity biotinylation enzyme, AirID, by using an algorithm to design an ancestral protein in silico based on huge genome sequence data. In this review, I will introduce an overview of BioID, TurboID and AirID, which are representative proximity biotinylation enzymes, and examples of protein interaction analysis using AirID mainly.

Journal

• Proteome Letters

  Proteome Letters 6 (1), 9-16, 2021

  Japanese Proteomics Society

Keywords

• AirID
• BioID
• mass spectrometry
• protein–protein interaction
• proximity biotinylation.

Details

• CRID: 1390570319884787072
• NII Article ID: 130008068499
• DOI: 10.14889/jpros.6.1_9
• ISSN: 24322776
• Text Lang: ja
• Data Source:
  • JaLC
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed