BAIT

TAF14

ANC1, SWP29, TAF30, TFG3, TATA-binding protein-associated factor TAF14, TafII30, L000000086, YPL129W
Subunit of TFIID, TFIIF, INO80, SWI/SNF, and NuA3 complexes; involved in RNA polymerase II transcription initiation and in chromatin modification; contains a YEATS domain
Saccharomyces cerevisiae (S288c)
PREY

GCN5

AAS104, ADA4, SWI9, histone acetyltransferase GCN5, KAT2, L000000684, YGR252W
Catalytic subunit of ADA and SAGA histone acetyltransferase complexes; modifies N-terminal lysines on histones H2B and H3; acetylates Rsc4p, a subunit of the RSC chromatin-remodeling complex, altering replication stress tolerance; relocalizes to the cytosol in response to hypoxia; mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay; greater involvement in repression of RNAPII-dependent transcription than in activation
Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

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

Shanle EK, Andrews FH, Meriesh H, McDaniel SL, Dronamraju R, DiFiore JV, Jha D, Wozniak GG, Bridgers JB, Kerschner JL, Krajewski K, Martin GM, Morrison AJ, Kutateladze TG, Strahl BD

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 ... [more]

Genes Dev. Sep. 01, 2015; 29(17);1795-800 [Pubmed: 26341557]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID