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http://purl.uniprot.org/citations/17314980http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17314980http://www.w3.org/2000/01/rdf-schema#comment"Defining the functional relationships between proteins is critical for understanding virtually all aspects of cell biology. Large-scale identification of protein complexes has provided one important step towards this goal; however, even knowledge of the stoichiometry, affinity and lifetime of every protein-protein interaction would not reveal the functional relationships between and within such complexes. Genetic interactions can provide functional information that is largely invisible to protein-protein interaction data sets. Here we present an epistatic miniarray profile (E-MAP) consisting of quantitative pairwise measurements of the genetic interactions between 743 Saccharomyces cerevisiae genes involved in various aspects of chromosome biology (including DNA replication/repair, chromatid segregation and transcriptional regulation). This E-MAP reveals that physical interactions fall into two well-represented classes distinguished by whether or not the individual proteins act coherently to carry out a common function. Thus, genetic interaction data make it possible to dissect functionally multi-protein complexes, including Mediator, and to organize distinct protein complexes into pathways. In one pathway defined here, we show that Rtt109 is the founding member of a novel class of histone acetyltransferases responsible for Asf1-dependent acetylation of histone H3 on lysine 56. This modification, in turn, enables a ubiquitin ligase complex containing the cullin Rtt101 to ensure genomic integrity during DNA replication."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.org/dc/terms/identifier"doi:10.1038/nature05649"xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Han J."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Krogan N.J."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Cheng B."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Brown G.W."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Ding H."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Berger S.L."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Maas N.L."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Schuldiner M."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Weissman J.S."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Andrews B."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Recht J."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Emili A."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Greenblatt J.F."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Hieter P."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Boone C."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Gebbia M."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Fillingham J."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Roguev A."xsd:string
http://purl.uniprot.org/citations/17314980http://purl.uniprot.org/core/author"Shales M."xsd:string