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. 2007 Apr 12;446(7137):806-10.
doi: 10.1038/nature05649. Epub 2007 Feb 21.

Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map

Sean R Collins  1 , Kyle M Miller, Nancy L Maas, Assen Roguev, Jeffrey Fillingham, Clement S Chu, Maya Schuldiner, Marinella Gebbia, Judith Recht, Michael Shales, Huiming Ding, Hong Xu, Junhong Han, Kristin Ingvarsdottir, Benjamin Cheng, Brenda Andrews, Charles Boone, Shelley L Berger, Phil Hieter, Zhiguo Zhang, Grant W Brown, C James Ingles, Andrew Emili, C David Allis, David P Toczyski, Jonathan S Weissman, Jack F Greenblatt, Nevan J Krogan
Affiliations

Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map

Sean R Collins et al. Nature. .

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.

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