title: In vivo protein-protein interaction studies with BiFC: conditions, cautions, and caveats.
abstract: Bimolecular fluorescence complementation (BiFC), performed with suitable controls and the right conditions, can be a straightforward and simple method to assess protein-protein interactions accessible to anyone with basic confocal microscopy skills. It is of course not without its own potential pitfalls and requires specific controls. Here we describe its use to study the interactions between pathogen effector proteins and host proteins inside plant cells.
authors.affiliation: Cell and Molecular Sciences, The James Hutton Institute, Errol Road, Invergowrie, Dundee, DD2 5DA, UK, Petra.Boevink@hutton.ac.uk.
authors.forename: Petra
authors.initials: P
authors.lastname: Boevink
authors.forename: Hazel
authors.initials: H
authors.lastname: McLellan
authors.forename: Tatyana
authors.initials: T
authors.lastname: Bukharova
authors.forename: Stefan
authors.initials: S
authors.lastname: Engelhardt
authors.forename: Paul
authors.initials: P
authors.lastname: Birch
mesh_terms: D060054:Agrobacterium / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005453:Fluorescence; D021621:Imaging, Three-Dimensional; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D014026:Nicotiana / Q000378:metabolism