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• W2126740537 abstract "The Rpd3S histone deacetylase complex represses cryptic transcription initiation within coding regions by maintaining the hypo-acetylated state of transcribed chromatin. Rpd3S recognizes methylation of histone H3 at lysine 36 (H3K36me), which is required for its deacetylation activity. Rpd3S is able to function over a wide range of H3K36me levels, making this a unique system to examine how chromatin regulators tolerate the reduction of their recognition signal. Here, we demonstrated that Rpd3S makes histone modification-independent contacts with nucleosomes, and that Rpd3S prefers di-nucleosome templates since two binding surfaces can be readily accessed simultaneously. Importantly, this multivalent mode of interaction across two linked nucleosomes allows Rpd3S to tolerate a two-fold intramolecular reduction of H3K36me. Our data suggest that chromatin regulators utilize an intrinsic di-nucleosome-recognition mechanism to prevent compromised function when their primary recognition modifications are diluted." @default.
• W2126740537 created "2016-06-24" @default.
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• W2126740537 date "2012-08-03" @default.
• W2126740537 modified "2023-10-09" @default.
• W2126740537 title "Multivalent di-nucleosome recognition enables the Rpd3S histone deacetylase complex to tolerate decreased H3K36 methylation levels" @default.
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• W2126740537 doi "https://doi.org/10.1038/emboj.2012.221" @default.
• W2126740537 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3433781" @default.
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• W2126740537 hasPublicationYear "2012" @default.
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