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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
Published on: February 16, 2015
The YEATS domain of Taf14 in Saccharomyces cerevisiae has a negative impact on cell growth
Julia M Schulze1, Caroline M Kane, Ana Ruiz-Manzano
1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
Abstract:
The role of a highly conserved YEATS protein motif is explored in the context of the Taf14 protein of Saccharomyces cerevisiae. In S. cerevisiae, Taf14 is a protein physically associated with many critical multisubunit complexes including the general transcription factors TFIID and TFIIF, the chromatin remodeling complexes SWI/SNF, Ino80 and RSC, Mediator and the histone modification enzyme NuA3. Taf14 is a member of the YEATS superfamily, conserved from bacteria to eukaryotes and thought to have a transcription stimulatory activity. However, besides its ubiquitous presence and its links with transcription, little is known about Taf14's role in the nucleus. We use structure-function and mutational analysis to study the function of Taf14 and its well conserved N-terminal YEATS domain. We show here that the YEATS domain is not necessary for Taf14's association with these transcription and chromatin remodeling complexes, and that its presence in these complexes is dependent only on its C-terminal domain. Our results also indicate that Taf14's YEATS domain is not necessary for complementing the synthetic lethality between TAF14 and the general transcription factor TFIIS (encoded by DST1). Furthermore, we present evidence that the YEATS domain of Taf14 has a negative impact on cell growth: its absence enables cells to grow better than wild-type cells under stress conditions, like the microtubule destabilizing drug benomyl. Moreover, cells expressing solely the YEATS domain grow worser than cells expressing any other Taf14 construct tested, including the deletion mutant. Thus, this highly conserved domain should be considered part of a negative regulatory loop in cell growth.
Insights
The YEATS domain of the Taf14 protein in yeast does not appear essential for its role in transcription complexes. Surprisingly, this conserved domain negatively impacts cell growth, especially under stress conditions.
Area of Science:
- Molecular Biology
- Yeast Genetics
- Protein Function Analysis
Background:
- Taf14 is a protein in Saccharomyces cerevisiae associated with crucial transcription and chromatin remodeling complexes.
- Taf14 belongs to the YEATS superfamily, a conserved group of proteins implicated in transcription regulation.
- The precise nuclear function of Taf14, particularly its conserved YEATS domain, remains largely uncharacterized.
Purpose of the Study:
- To investigate the functional role of the conserved N-terminal YEATS domain of the Taf14 protein.
- To determine the contribution of the YEATS domain to Taf14's association with protein complexes and its role in cell viability.
Main Methods:
- Structure-function analysis of the Taf14 protein.
- Site-directed mutagenesis to create Taf14 variants.
- Assays for protein complex association, complementation of synthetic lethality, and cell growth under stress conditions.
Main Results:
- The YEATS domain is not required for Taf14's association with transcription and chromatin remodeling complexes; this interaction depends on the C-terminal domain.
- The YEATS domain is dispensable for complementing the synthetic lethality between TAF14 and the general transcription factor TFIIS.
- Absence of the YEATS domain enhances cell growth under stress conditions (e.g., benomyl treatment), suggesting a negative regulatory role.
Conclusions:
- The conserved YEATS domain of Taf14 is not essential for its participation in major nuclear complexes or for overcoming specific genetic lethality.
- The YEATS domain appears to negatively regulate cell growth, particularly under environmental stress.
- This conserved domain may function as part of a negative regulatory loop influencing cell growth dynamics in yeast.
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