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Functions of SAGA in development and disease.

ABSTRACT: Precise regulation of gene expression programs during embryo development requires cooperation between transcriptional factors and histone-modifying enzymes, such as the Gcn5 histone acetyltransferase. Gcn5 functions within a multi-subunit complex, called SAGA, that is recruited to specific genes through interactions with sequence-specific DNA-binding proteins to aid in gene activation. Although the transcriptional programs regulated by SAGA in embryos are not well defined, deletion of either Gcn5 or USP22, the catalytic subunit of a deubiquitinase module in SAGA, leads to early embryonic lethality. Here, we review the known functions of Gcn5, USP22 and associated proteins during development and discuss how these functions might be related to human disease states, including cancer and neurodegenerative diseases.

SUBMITTER: Wang L

PROVIDER: S-EPMC4159956 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Functions of SAGA in development and disease.

Wang Li L Dent Sharon Y R SY

Epigenomics 20140601 3

Precise regulation of gene expression programs during embryo development requires cooperation between transcriptional factors and histone-modifying enzymes, such as the Gcn5 histone acetyltransferase. Gcn5 functions within a multi-subunit complex, called SAGA, that is recruited to specific genes through interactions with sequence-specific DNA-binding proteins to aid in gene activation. Although the transcriptional programs regulated by SAGA in embryos are not well defined, deletion of either Gcn ...[more]

PMID: 25111486

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Project description:MudPIT analyses of novel spliceosomal SF3B component in SAGA complex Stable Drosophila S2 cell lines expressing SF3B5 (CG11985, NP_652189.1), U2B (SNF; CG4528, NP_511045.1), Ada2b-PB (CG9638, NP_001027151.1), Spt3 (CG3169, NP_650146.1), Spt20 (CG17689, NP_648659.2), ATXN7 (CG9866, NP_722803.1), Ada1 (CG31866, NP_723703.1), SAF6 (CG3883, NP_608545.1), Sgf29 (CG30390, NP_726051.1), and WDA (CG4448, NP_651136.1) in the pRmHa3-CHA2FL2 vector were generated as described (Guelman S, et al., Mol Cell Biol. 2006;26:7178-89). Protein complexes were purified by tandem FLAG-HA affinity purification as described (Weake VM, et al. Genes Dev. 2009;23:2818-23). Two negative controls were purified in parallel from S2 cells without any vectors and from S2 cells expressing CG6459. Where indicated, 250 ug/mL RNAseA was added to soluble nuclear extract from WDA-expressing cells prior to immunoprecipitation. Proteins were digested with endoproteinase LysC followed by trypsin. The resulting peptide mixtures were analyzed by Multidimensional Protein Identification Technology (MudPIT) on an LTQ ion trap mass spectrometer as described (Florens L, Washburn MP. Methods Mol Biol 2006;328:159-75). RAW files were extracted into .ms2 file format using RawDistiller v. 1.0 (in-house developed software). The MS/MS spectra were searched using SEQUEST v.27 (rev.9) with a peptide mass tolerance of 3 amu and of +/- 0.5 amu for fragment ions. No enzyme specificity was imposed during the SEQUEST searches against a protein database containing 18425 non-redundant Drosophila melanogaster proteins (NCBI 2011-04-11 release), as well as 177 usual contaminants such as human keratins, IgGs and proteolytic enzymes. To estimate false discovery rates (FDR), each protein sequence was randomized (keeping the same amino acid composition and length) and the resulting "shuffled" sequences were added to the database used for the SEQUEST searches, for a total search space of 37204 amino acid sequences. To account for alkylation by CAM, 57.02146 Da were added statically to cysteine residues for all searches.

Dataset Information

Functions of SAGA in development and disease.

Publications

Functions of SAGA in development and disease.

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