ArticleBMC genetics2008
Systematic genetic array analysis links the Saccharomyces cerevisiae SAGA/SLIK and NuA4 component Tra1 to multiple cellular processes.
Article in BMC genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 33 citations in OpenAlex.
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- Csn5 Depletion Reverses Mitochondrial Defects in GCN5-NullInternational journal of molecular sciences · 2025Article
- The MYB-like protein MylA contributes to conidiogenesis and conidial germination in Aspergillus nidulans.Communications biology · 2024Article
- Evolutionary diversity of the control of the azole response by Tra1 across yeast species.G3 (Bethesda, Md.) · 2024Article
- Tra1 controls the transcriptional landscape of the aging cell.G3 (Bethesda, Md.) · 2023Article
- The SAGA and NuA4 component Tra1 regulates Candida albicans drug resistance and pathogenesis.Genetics · 2021Article
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- The Pseudokinase Domain ofG3 (Bethesda, Md.) · 2018Article
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- Genetic selection for mistranslation rescues a defective co-chaperone in yeast.Nucleic acids research · 2017Article
- Quantitative phosphoproteomic profiling of fiber differentiation and initiation in a fiberless mutant of cotton.BMC genomics · 2014Article
- Genetic evidence links the ASTRA protein chaperone component Tti2 to the SAGA transcription factor Tra1.Genetics · 2012Article
- Loss of nonsense mediated decay suppresses mutations in Saccharomyces cerevisiae TRA1.BMC genetics · 2012Article
- Phosphorylation of Mcm2 modulates Mcm2-7 activity and affects the cell's response to DNA damage.Nucleic acids research · 2011Article
- MYST-family histone acetyltransferases: beyond chromatin.Cellular and molecular life sciences : CMLS · 2011Review
- Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4.PloS one · 2011Article
- Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1.Current genetics · 2010Article
- Identification of Pep4p as the protease responsible for formation of the SAGA-related SLIK protein complex.The Journal of biological chemistry · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTra1 is an essential 437-kDa component of the Saccharomyces cerevisiae SAGA/SLIK and NuA4 histone acetyltransferase complexes. It is a member of a group of key signaling molecules that share a carboxyl-terminal domain related to phosphatidylinositol-3-kinase but unlike many family members, it lacks kinase activity. To identify genetic interactions for TRA1 and provide insight into its function we have performed a systematic genetic array analysis (SGA) on tra1SRR3413, an allele that is defective in transcriptional regulation.
resultsThe SGA analysis revealed 114 synthetic slow growth/lethal (SSL) interactions for tra1SRR3413. The interacting genes are involved in a range of cellular processes including gene expression, mitochondrial function, and membrane sorting/protein trafficking. In addition many of the genes have roles in the cellular response to stress. A hierarchal cluster analysis revealed that the pattern of SSL interactions for tra1SRR3413 most closely resembles deletions of a group of regulatory GTPases required for membrane sorting/protein trafficking. Consistent with a role for Tra1 in cellular stress, the tra1SRR3413 strain was sensitive to rapamycin. In addition, calcofluor white sensitivity of the strain was enhanced by the protein kinase inhibitor staurosporine, a phenotype shared with the Ada components of the SAGA/SLIK complex. Through analysis of a GFP-Tra1 fusion we show that Tra1 is principally localized to the nucleus.
conclusionWe have demonstrated a genetic association of Tra1 with nuclear, mitochondrial and membrane processes. The identity of the SSL genes also connects Tra1 with cellular stress, a result confirmed by the sensitivity of the tra1SRR3413 strain to a variety of stress conditions. Based upon the nuclear localization of GFP-Tra1 and the finding that deletion of the Ada components of the SAGA complex result in similar phenotypes as tra1SRR3413, we suggest that the effects of tra1SRR3413 are mediated, at least in part, through its role in the SAGA complex.
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