Abstract

Repression of yeast a cell-specific genes by the global repressor Ssn6/Tup1 has been linked to a specific organization of chromatin. We report here that Tup1 directly interacts with the amino-terminal tails of histones H3 and H4, providing a molecular basis for this connection. This interaction appears to be required for Tup1 function because amino-terminal mutations in H3 and H4 that weaken interactions with Tup1 cause derepression of both a cell-specific and DNA damage-inducible genes. Moreover, the Tup1 histone-binding domain coincides with the previously defined Tup1 repression domain. Tup1/histone interactions are negatively influenced by high levels of histone acetylation, suggesting a mechanism whereby the organization of chromatin may be modulated in response to changing environmental signals.

Keywords

DerepressionBiologyChromatinHistoneRepressorHistone H3Psychological repressionHistone H4AcetylationCell biologyPRC2Histone H2AGeneticsSaccharomyces cerevisiaeHistone codeYeastGeneGene expressionNucleosome

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Publication Info

Year
1996
Type
article
Volume
10
Issue
10
Pages
1247-1259
Citations
453
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Closed

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Diane G. Edmondson, M. Mitchell Smith, Sharon Y. Roth (1996). Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.. Genes & Development , 10 (10) , 1247-1259. https://doi.org/10.1101/gad.10.10.1247

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DOI
10.1101/gad.10.10.1247