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Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.
The bromodomain: a chromatin-targeting module?
The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo.
Cell-cycle perturbations suppress the slow-growth defect of spt10? mutants in Saccharomyces cerevisiae.
Redundant roles for the TFIID and SAGA complexes in global transcription.
Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex.
Evidence that Spt10 and Spt21 of Saccharomyces cerevisiae play distinct roles in vivo and functionally interact with MCB-binding factor, SCB-binding factor and Snf1.
Specific components of the SAGA complex are required for Gcn4- and Gcr1-mediated activation of the his4-912delta promoter in Saccharomyces cerevisiae.
Spt10 and Spt21 are required for transcriptional silencing in Saccharomyces cerevisiae.
Spt10-dependent transcriptional activation in Saccharomyces cerevisiae requires both the Spt10 acetyltransferase domain and Spt21.
The nucleosome remodeling complex, Snf/Swi, is required for the maintenance of transcription in vivo and is partially redundant with the histone acetyltransferase, Gcn5.
SPT10 and SPT21 are required for transcription of particular histone genes in Saccharomyces cerevisiae.
The SPT10 and SPT21 genes of Saccharomyces cerevisiae.
The Hog1 mitogen-activated protein kinase mediates a hypoxic response in Saccharomyces cerevisiae.
The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4.
Molecular architecture of the S. cerevisiae SAGA complex.