Multi-tasking on chromatin with the SAGA coactivator complexes.
Open accessAbstract
Over the past 10 years, much progress has been made to understand the roles of the similar, yet distinct yeast SAGA and SLIK coactivator complexes involved in histone post-translational modification and gene regulation. Many different groups have elucidated functions of the SAGA complexes including identification of novel components, which have conferred additional distinct functions. Together, recent studies demonstrate unique attributes of the SAGA coactivator complexes in histone acetylation, methylation, phosphorylation, and deubiquitination. In addition to roles in transcriptional activation with the 19S proteasome regulatory particle, recent evidence also suggests functions for SAGA in elongation and mRNA export. The modular nature of SAGA allows this approximately 1.8 MDa complex to organize its functions and carry out multiple roles during transcription, particularly under conditions of cellular stress.
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ADA2 is a component of the SAGA complex, which plays an important role in histone acetylation and is involved in the regulation of numerous genes.
“ADA2 is a component of the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex, which plays an important role in histone acetylation and is involved in the regulation of numerous genes (Wang et al., 1998; Daniel and Grant, 2007).”
From A Potential Antifungal Effect of Chitosan Against Candida albicans Is Mediated via the Inhibition of SAGA Complex Component Expression and the Subsequent Alteration of Cell Surface Integrity (2019) · cites this paper as Daniel and Grant, 2007
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References 151 · Cited by 111
- Authors
- Daniel, J. A., & Grant, P. A.
- Affiliations
- University of Virginia (US)
- Corresponding author
- Grant, Patrick A.
- ORCID
- Daniel, Jeremy A.
- Venue
- Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
- Publisher
- Elsevier BV
- Published
- 2007-05
- Volume
- 618
- Issue
- 1-2
- Pages
- 135-148
- ISSN
- 0027-5107 (ISSN-L)
- 1386-1964
- PMC
- PMC1892243
- OpenAlex
- W1978077699
- Cited by
- 111
- References
- 151
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 7 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 4 · 2016: 3 · 2015: 5 · 2014: 7 · 2013: 9 · 2012: 6
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Mutation research. Fundamental and molecular mechanisms of mutagenesis (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (DK58646, NS049065)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- histone modifications, histone acetylation, histone methylation, histone phosphorylation, histone deubiquitination, transcriptional activation, 19S proteasome, transcription elongation, mRNA export, cellular stress, chromatin regulation, Saccharomyces cerevisiae
- MeSH terms
- Acetyltransferases, Animals, Chromatin, Fungal Proteins, Histones, Humans, Models, Biological, Mutation, Protein Binding, Protein Conformation, Saccharomyces cerevisiae, Substrate Specificity, Transcription, Genetic, DNA Methylation, Ubiquitin
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