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17 April 2024 |
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Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map | | Sean R Collins
; 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
; | | Date: |
12 Apr 2007 | | Journal: | Nature, 446 (7137), 806-10 | | 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. | | Source: | PubMed, pmid17314980 doi: 10.1038/nature05649 | | Services: | Forum | Review | Favorites | |
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