Validation of Nuclear Pore Complex Protein-Protein Interactions by Transient Expression in Plants

Fumika Ikeda; Kentaro Tamura

doi:10.1007/978-1-0716-2337-4_15

Validation of Nuclear Pore Complex Protein-Protein Interactions by Transient Expression in Plants

Methods Mol Biol. 2022:2502:235-243. doi: 10.1007/978-1-0716-2337-4_15.

Authors

Fumika Ikeda¹, Kentaro Tamura²

Affiliations

¹ Department of Environmental and Life Sciences, School of Food and Nutritional Sciences, University of Shizuoka, Shizuoka, Japan.
² Department of Environmental and Life Sciences, School of Food and Nutritional Sciences, University of Shizuoka, Shizuoka, Japan. tamura@u-shizuoka-ken.ac.jp.

PMID: 35412242
DOI: 10.1007/978-1-0716-2337-4_15

Abstract

The nuclear pore complex (NPC) is the largest protein complex, consisting of multiple copies of over 30 different nucleoporins. The interactions between the nucleoporins are critical elements for the NPC functions of the nuclear envelope in plant cells. In recent years, transient expression-based validations of protein-protein interactions have been widely used in plants. Bimolecular fluorescence complementation assay and coimmunoprecipitation assays are powerful tools to identify the molecules that interact with specific proteins. Here, as an example, we describe these techniques using nucleoporin protein interactions in plants.

Keywords: Agroinfiltration; Arabidopsis thaliana; Bimolecular fluorescence complementation; Coimmunoprecipitation; Nicotiana benthamiana; Nicotiana tabacum; Nuclear pore complex.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Nuclear Envelope / metabolism
Nuclear Pore Complex Proteins* / genetics
Nuclear Pore Complex Proteins* / metabolism
Nuclear Pore* / metabolism
Plants / metabolism

Substances

Nuclear Pore Complex Proteins