@inbook{4f73c6cee6d44a4d91639ac061c22c5a,
title = "Using the yeast two-hybrid system to identify protein-protein interactions",
abstract = "The yeast two-hybrid system is currently one of the most standardized protein interaction mapping techniques. The rationale of the yeast two-hybrid system relies on the physical separation of the DNA-binding domain from the transcriptional activation domain of several transcription factors. The protein of interest (bait) is fused to a DNA-binding domain, and complementary DNA (cDNA) library-encoded proteins are fused to a transcriptional activation domain. When a protein encoded by the cDNA library binds to the bait, both activities of the transcription factor are rejoined resulting in transcription from a reporter gene. Here, we describe protocols to test interactions between two individual proteins and to look for novel interacting partners by screening a single protein or domain against a library of other proteins using a GAL4 based yeast two-hybrid system.",
keywords = "GAL4, Interactome, Interactors, Protein-protein interaction, Two-hybrid system, Yeast",
author = "Edgar Rodr{\'i}guez-Negrete and Bejarano, {Eduardo R.} and Castillo, {Araceli G.}",
year = "2014",
doi = "10.1007/978-1-62703-631-3_18",
language = "Ingl{\'e}s",
isbn = "9781627036306",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "241--258",
booktitle = "Plant Proteomics",
}