Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map.
Nature
; 446(7137): 806-10, 2007 Apr 12.
Article
en En
| MEDLINE
| ID: mdl-17314980
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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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Cromosomas Fúngicos
/
Proteínas de Saccharomyces cerevisiae
/
Complejos Multiproteicos
/
Epistasis Genética
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Nature
Año:
2007
Tipo del documento:
Article
País de afiliación:
Estados Unidos