title: Use of bimolecular fluorescence complementation in yeast Saccharomyces cerevisiae.
abstract: Visualization of protein-protein interactions in vivo offers a powerful tool to resolve spatial and temporal aspects of cellular functions. Bimolecular fluorescence complementation (BiFC) makes use of nonfluorescent fragments of green fluorescent protein or its variants that are added as "tags" to target proteins under study. Only upon target protein interaction is a fluorescent protein complex assembled and the site of interaction can be monitored by microscopy. In this chapter, we describe the method and tools for use of BiFC in the yeast Saccharomyces cerevisiae.
authors.affiliation: Institute of Biotechnology, University of Helsinki, Finland.
authors.forename: Kari-Pekka
authors.initials: KP
authors.lastname: Skarp
authors.forename: Xueqiang
authors.initials: X
authors.lastname: Zhao
authors.forename: Marion
authors.initials: M
authors.lastname: Weber
authors.forename: Jussi
authors.initials: J
authors.lastname: Jantti
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D005800:Genes, Fungal; D008163:Luminescent Measurements / Q000379:methods*; D008164:Luminescent Proteins / Q000378:metabolism; D008853:Microscopy; D008969:Molecular Sequence Data; D010957:Plasmids / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D014170:Transformation, Genetic
chemical_list: D001426:Bacterial Proteins; D008164:Luminescent Proteins; C054562:yellow fluorescent protein, Bacteria