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WI‐PHI: A weighted yeast interactome enriched for direct physical interactions
Author(s) -
Kiemer Lars,
Costa Stefano,
Ueffing Marius,
Cesareni Gianni
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200600448
Subject(s) - interactome , yeast , computational biology , proteome , tandem affinity purification , proteomics , heuristic , computer science , protein–protein interaction , scale (ratio) , probabilistic logic , saccharomyces cerevisiae , biology , interaction network , systems biology , data mining , bioinformatics , genetics , artificial intelligence , gene , biochemistry , physics , quantum mechanics , affinity chromatography , enzyme
How is the yeast proteome wired? This important question, central in yeast systems biology, remains unanswered in spite of the abundance of protein interaction data from high‐throughput experiments. Unfortunately, these large‐scale studies show striking discrepancies in their results and coverage such that biologists scrutinizing the “interactome” are often confounded by a mix of established physical interactions, functional associations, and experimental artifacts. This stimulated early attempts to integrate the available information and produce a list of protein interactions ranked according to an estimated functional reliability. The recent publication of the results of two large protein interaction experiments and the completion of a comprehensive literature curation effort has more than doubled the available information on the wiring of the yeast proteome. This motivates a fresh approach to the compilation of a yeast interactome based purely on evidence of physical interaction. We present a procedure exploiting both heuristic and probabilistic strategies to draft the yeast interactome taking advantage of various heterogeneous data sources: application of tandem affinity purification coupled to MS (TAP‐MS), large‐scale yeast two‐hybrid studies, and results of small‐scale experiments stored in dedicated databases. The end result is WI‐PHI, a weighted network encompassing a large majority of yeast proteins.