Transcriptomics,Multiomics

Dataset Information

4

Association of Taf14 with acetylated histone H3 directs the DNA damage response and gene transcription


ABSTRACT: We sequenced mRNA from triplicate log-phase cultures of BY4741 (WT) transformed with pRS313-HA3-SSN6 and taf14D transformed with pRS313-HA3-SSN6 (empty vector), full-length pRS313-TAF14-HA3-SSN6, or pRS313-taf14W81A-HA3-SSN6 cultured in synthetic complete media lacking histidine. Examination of changes in gene expression when the YEATS domain of Taf14 is mutated so it cannot bind acetyl-H3.

OTHER RELATED OMICS DATASETS IN: PRJNA292038

ORGANISM(S): Saccharomyces cerevisiae  

SUBMITTER: B D Strahl   Erin K Shanle  E K Shanle 

PROVIDER: E-GEOD-71768 | ArrayExpress | 2015-09-09

SECONDARY ACCESSION(S): GSE71768SRP062085PRJNA292038

REPOSITORIES: GEO, ArrayExpress, ENA

Dataset's files

Source:
Action DRS
E-GEOD-71768.additional.1.zip Other
E-GEOD-71768.idf.txt Idf
E-GEOD-71768.sdrf.txt Txt
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Publications


The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcrip  ...[more]

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