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Functional organization of the yeast proteome by systematic analysis of protein complexes
TLDR
The analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions, which contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery. Expand
A generic protein purification method for protein complex characterization and proteome exploration
TLDR
A generic procedure to purify proteins expressed at their natural level under native conditions using a novel tandem affinity purification (TAP) tag and Combined with mass spectrometry, the TAP strategy allows for the identification of proteins interacting with a given target protein. Expand
The tandem affinity purification (TAP) method: a general procedure of protein complex purification.
TLDR
The TAP method is developed as a tool that allows rapid purification under native conditions of complexes, even when expressed at their natural level, and is a very useful procedure for protein purification and proteome exploration. Expand
Cryptic Pol II Transcripts Are Degraded by a Nuclear Quality Control Pathway Involving a New Poly(A) Polymerase
TLDR
It is shown here that several supposedly silent intergenic regions in the genome of S. cerevisiae are actually transcribed by RNA polymerase II, suggesting that the expressed fraction of the genome is higher than anticipated. Expand
Cytoplasmic foci are sites of mRNA decay in human cells
TLDR
The occurrence of 5′–3′ mRNA decay in specific subcellular locations in human cells suggests that the cytoplasm of eukaryotic cells may be more organized than previously anticipated. Expand
A single subunit, Dis3, is essentially responsible for yeast exosome core activity
TLDR
It is observed that the yeast exosome ring mediates interactions with protein partners, providing an explanation for its essential function. Expand
A Sm‐like protein complex that participates in mRNA degradation
TLDR
Results indicate the involvement of a new conserved Sm‐like protein complex and a new factor, Pat1p, in mRNA degradation and suggest a physical connection between decapping and exonuclease trimming. Expand
Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA
TLDR
The crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic is presented. Expand
The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program.
Set3 is one of two proteins in the yeast Saccharomyces cerevisiae that, like Drosophila Trithorax, contains both SET and PHD domains. We found that Set3 forms a single complex, Set3C, with Snt1,Expand
REF, an evolutionary conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export.
TLDR
Yra1p and members of the REF family of hnRNP-like proteins may facilitate the interaction of TAP/Mex67p with cellular mRNAs, which is likely to be mediated by protein-protein interactions. Expand
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