Abstract:
: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.
journal_name
Naturejournal_title
Natureauthors
Collins SR,Miller KM,Maas NL,Roguev A,Fillingham J,Chu CS,Schuldiner M,Gebbia M,Recht J,Shales M,Ding H,Xu H,Han J,Ingvarsdottir K,Cheng B,Andrews B,Boone C,Berger SL,Hieter P,Zhang Z,Brown GW,Ingles CJ,Emilidoi
10.1038/nature05649subject
Has Abstractpub_date
2007-04-12 00:00:00pages
806-10issue
7137eissn
0028-0836issn
1476-4687pii
nature05649journal_volume
446pub_type
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