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Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
TLDR
T tandem affinity purification was used to process 4,562 different tagged proteins of the yeast Saccharomyces cerevisiae to identify protein–protein interactions, which will help future studies on individual proteins as well as functional genomics and systems biology.
Global Mapping of the Yeast Genetic Interaction Network
TLDR
Because digenic interactions are common in yeast, similar networks may underlie the complex genetics associated with inherited phenotypes in other organisms.
Toward a Comprehensive Atlas of the Physical Interactome of Saccharomyces cerevisiae*S
TLDR
A novel probabilistic metric is created that takes advantage of the high density of data, including both the presence and absence of individual associations, to provide a measure of the relative confidence of each potential protein-protein interaction and organized proteins into coherent multisubunit complexes using hierarchical clustering.
Interaction network containing conserved and essential protein complexes in Escherichia coli
TLDR
Insight is provided into the function of previously uncharacterized bacterial proteins and the overall topology of a microbial interaction network, the core components of which are broadly conserved across Prokaryota.
A Bayesian Networks Approach for Predicting Protein-Protein Interactions from Genomic Data
TLDR
This work develops an approach using Bayesian networks to predict protein-protein interactions genome-wide in yeast, and observes that at given levels of sensitivity, the predictions are more accurate than the existing high-throughput experimental data sets.
The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II
TLDR
It is shown that Rtt103 and the Rat1/Rai1 5′ → 3′ exonuclease are localized at 3′ ends of protein coding genes, supporting a model in which poly(A) site cleavage and subsequent degradation of the 3′-downstream RNA by Rat1 trigger transcription termination.
The C-terminal domain of RNA polymerase II couples mRNA processing to transcription
TLDR
It is shown that the carboxy-terminal domain of the pol II large subunit is required for efficient RNA processing, and an association between the CTD and 3′-processing factors suggests that an mRNA 'factory' exists which carries out coupled transcription, splicing and cleavage–polyadenylation of mRNA precursors.
RNA Polymerase II Elongation Factors of Saccharomyces cerevisiae: a Targeted Proteomics Approach
TLDR
To physically characterize the web of interactions connecting the Saccharomyces cerevisiae proteins suspected to be RNA polymerase II elongation factors, subunits of Spt4/Spt5 and Spt16/Pob3 were affinity purified under conditions designed to minimize loss of associated polypeptides and then identified by mass spectrometry.
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