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The yeast histone deacetylase Rpd3 can be recruited to promoters to repress transcription initiation. Biochemical, genetic, and gene-expression analyses show that Rpd3 exists in two distinct complexes. The smaller complex, Rpd3C(S), shares Sin3 and Ume1 with Rpd3C(L) but contains the unique subunits Rco1 and Eaf3. Rpd3C(S) mutants exhibit phenotypes(More)
As RNA polymerase II (RNApII) transitions from initiation to elongation, Mediator and the basal transcription factors TFIID, TFIIA, TFIIH, and TFIIE remain at the promoter as part of a scaffold complex, whereas TFIIB and TFIIF dissociate. The yeast Ctk1 kinase associates with elongation complexes and phosphorylates serine 2 in the YSPTSPS repeats of the(More)
Epigenetic changes in chromatin state are associated with aging. Notably, two histone modifications have recently been implicated in lifespan regulation, namely acetylation at H4 lysine 16 in yeast and methylation at H3 lysine 4 (H3K4) in nematodes. However, less is known about other histone modifications. Here, we report that cellular aging is associated(More)
Nucleolar ribosomal DNA is tightly associated with silent heterochromatin, which is important for rDNA stability, nucleolar integration and cellular senescence. Two pathways have been described that lead to rDNA silencing in yeast: 1) the RENT (regulator of nucleolar silencing and telophase exit) complex, which is composed of Net1, Sir2 and Cdc14 and is(More)
The post-translational modification of histones has been implicated in the regulation of cellular lifespan. Previously, we reported that cellular aging is associated with increased ubiquitylation of histone H2B and methylation of histone H3 at lysines 4 and 79 in yeast telomeric heterochromatin. Here, we show the antagonistic role of Set2 methyltransferase,(More)
In budding yeast, a highly conserved heterodimeric protein complex that is composed of the Rpb4 and Rpb7 proteins within RNA polymerase II shuttles between the nucleus and cytoplasm where it coordinates various steps of gene expression by associating with mRNAs. Although distinct stages of gene expression potentially contribute to the regulation of cellular(More)
Endosomal sorting complex required for transport (ESCRT) is involved in membrane protein degradation through the recognition and sorting of ubiquitylated cargo proteins into the multivesicular body before fusion with the lysosome/vacuole. However, recent studies have challenged this canonical cellular function of ESCRT and have implicated a role for this(More)
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