title: Detecting protein-protein interactions with the Split-Ubiquitin sensor.
abstract: A detailed understanding of a cellular process requires the knowledge about the interactions between its protein constituents. The Split-Ubiquitin technique allows to monitor and detect interactions of very diverse proteins, including transcription factors and membrane-associated proteins. The technique is based on unique features of ubiquitin, the enzymes of the ubiquitin pathway, and the reconstitution of a native-like ubiquitin from its N- and C-terminal fragments. Using Ura3p as a reporter for the reconstitution of the ubiquitin fragments, methods are presented that enable to screen in yeast for interaction partners of a given protein with either a randomly generated expression library or a defined but more limited array of protein fusions.
authors.affiliation: Department of Biology, Institute of Molecular Genetics and Cell Biology, Ulm University, Ulm, Germany.
authors.forename: Alexander
authors.initials: A
authors.lastname: Dünkler
authors.forename: Judith
authors.initials: J
authors.lastname: Müller
authors.forename: Nils
authors.initials: N
authors.lastname: Johnsson
mesh_terms: D015374:Biosensing Techniques / Q000379:methods*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D060066:Protein Interaction Maps; D011506:Proteins / Q000032:analysis / Q000378:metabolism*; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011506:Proteins; D025801:Ubiquitin