Abstract
BackgroundThe YEATS domain is a highly conserved protein structure that interacts with acetylated and crotonylated lysine residues in N-terminal tails of histones. The budding yeast genome encodes three YEATS domain proteins (Taf14, Yaf9, and Sas5) that are all the subunits of different complexes involved in histone acetylation, gene transcription, and chromatin remodeling. As the strains deficient in all these three genes are inviable, it has been proposed that the YEATS domain is essential in yeast. In this study we investigate in more detail the requirement of YEATS domain proteins for yeast survival and the possible roles of Taf14 YEATS domain in the regulation of gene transcription.ResultsWe found that YEATS domains are not essential for the survival of Saccharomyces cerevisiae cells. Although the full deletion of all YEATS proteins is lethal in yeast, we show that the viability of cells can be restored by the expression of the YEATS-less version of Taf14 protein. We also explore the in vivo functions of Taf14 protein and show that the primary role of its YEATS domain is to stabilize the transcription pre-initiation complex (PIC). Our results indicate that Taf14-mediated interactions become crucial for PIC formation in rpb9Δ cells, where the recruitment of TFIIF to the PIC is hampered. Although H3 K9 residue has been identified as the interaction site of the Taf14 YEATS domain in vitro, we found that it is not the only interaction target in vivo.ConclusionsLethality of YEATS-deficient cells can be rescued by the expression of truncated Taf14 protein lacking the entire YEATS domain, indicating that the YEATS domains are not required for cell survival. The YEATS domain of Taf14 participates in PIC stabilization and acetylated/crotonylated H3K9 is not the critical target of the Taf14 YEATS domain in vivo.
Highlights
The YEATS domain is a highly conserved protein structure that interacts with acetylated and crotonylated lysine residues in N-terminal tails of histones
Mutant Taf14 protein without the YEATS domain ( Taf14ΔYEATS) lacks amino acids 6–121 and mutant Taf14 protein with a non-functional YEATS domain (taf14W81A) has substitution of Trp81 to alanine. b Tenfold serial dilutions of cells with single or double-knockout of TAF14, YAF9 and SAS5 were spotted onto synthetic complete (SC) plates and grown at 30 °C for 2 days. c Tenfold serial dilutions of taf14ΔYEATS or taf14W81A cells combined with YAF9 and SAS5 deletions
We hypothesized that the cause of lethality for mutant yeast strain lacking both TAF14 and YAF9 was not the absence of the YEATS domain as such, but rather the inability of taf14Δ strain to cope with extra stress resulting from deletion of YAF9
Summary
The YEATS domain is a highly conserved protein structure that interacts with acetylated and crotonylated lysine residues in N-terminal tails of histones. The budding yeast genome encodes three YEATS domain proteins (Taf, Yaf, and Sas5) that are all the subunits of different complexes involved in histone acetylation, gene transcription, and chromatin remodeling. The subunit of TFIIF, TFIID, INO80, SWI/SNF, and NuA3 complexes, was first shown to have the strongest interaction with H3K9ac peptides [12], but subsequent studies specified crotonylated H3K9 (H3K9cr) as its preferred binding target [13]. Structural analysis of the Taf YEATS domain revealed that Phe and Trp residues of the protein form an aromatic cage, which is required for Taf binding to the acetylated H3K9. Mutation of Trp to alanine in the YEATS domain is sufficient to abolish this interaction completely [12]
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