Protein-Protein Interactions Visualized by Bimolecular Fluorescence Complementation in Arabidopsis thaliana Protoplasts from Leaf

Methods Mol Biol. 2024:2787:305-313. doi: 10.1007/978-1-0716-3778-4_21.

Abstract

Bimolecular fluorescence complementation (BiFC) is a powerful tool for studying protein-protein interactions in living cells. By fusing interacting proteins to fluorescent protein fragments, BiFC allows visualization of spatial localization patterns of protein complexes. This method has been adapted to a variety of expression systems in different organisms and is widely used to study protein interactions in plant cells. The Agrobacterium-mediated transient expression protocol for BiFC assays in Nicotiana benthamiana (N. benthamiana) leaf cells is widely used, but in this chapter, a method for BiFC assay using Arabidopsis thaliana protoplasts is presented.

Keywords: Arabidopsis thaliana; BiFC; Protein-protein Interactions; Protoplast.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agrobacterium / genetics
  • Agrobacterium / metabolism
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Arabidopsis* / genetics
  • Arabidopsis* / metabolism
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Microscopy, Fluorescence / methods
  • Nicotiana / genetics
  • Nicotiana / metabolism
  • Plant Leaves* / genetics
  • Plant Leaves* / metabolism
  • Protein Binding
  • Protein Interaction Mapping / methods
  • Protoplasts* / metabolism

Substances

  • Arabidopsis Proteins
  • Luminescent Proteins