2007
DOI: 10.1186/gb-2007-8-6-r119
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The Sas3p and Gcn5p histone acetyltransferases are recruited to similar genes

Abstract: A macroarray platform was used to identify binding sites of yeast histone acetyltransferase catalytic subunits and to correlate their positions with acetylation of lysine 14 of histone H3, revealing that Sas3p and Gcn5p are recruited to similar sets of intensely transcribed genes.

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Cited by 42 publications
(55 citation statements)
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“…Our findings demonstrate that GAS1 has striking yet distinct genetic interactions with genes encoding the lysine acetyltransferases Gcn5 and Sas3, which themselves are synthetically lethal and have overlapping nucleosomal substrates (Howe et al 2001) and genome-wide localization patterns (Rosaleny et al 2007). Whereas the gas1 gcn5 double mutant is dead, there is mutual suppression of specific phenotypes in the gas1 sas3 strain.…”
Section: Discussionmentioning
confidence: 89%
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“…Our findings demonstrate that GAS1 has striking yet distinct genetic interactions with genes encoding the lysine acetyltransferases Gcn5 and Sas3, which themselves are synthetically lethal and have overlapping nucleosomal substrates (Howe et al 2001) and genome-wide localization patterns (Rosaleny et al 2007). Whereas the gas1 gcn5 double mutant is dead, there is mutual suppression of specific phenotypes in the gas1 sas3 strain.…”
Section: Discussionmentioning
confidence: 89%
“…In addition to the synthetic lethality, Gcn5 and Sas3 have overlapping sites of genomic localization (Rosaleny et al 2007) and share nucleosomal substrates (Howe et al 2001). Based on the similarities between Gcn5 and Sas3, we chose to analyze the gas1 sas3 double mutant to determine if the synthetic lethality observed with gas1 gcn5 was gene specific.…”
Section: Resultsmentioning
confidence: 99%
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