Structure of the transcription activator target Tra1 within the chromatin modifying complex SAGA
| Autor: | Adam Ben Shem, Annick Dejaegere, Alexandre Durand, Patrick Schultz, Grigory Sharov, Gabor Papai, Alexander G. Myasnikov, Karine Voltz, Olga Kolesnikova |
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| Přispěvatelé: | Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Models Molecular Protein subunit Science [SDV]Life Sciences [q-bio] General Physics and Astronomy General Biochemistry Genetics and Molecular Biology Article Fungal Proteins 03 medical and health sciences Protein Domains Transcription (biology) Coactivator Humans Acetyltransferase complex Amino Acid Sequence lcsh:Science Histone Acetyltransferases Multidisciplinary Sequence Homology Amino Acid Chemistry Activator (genetics) Cryoelectron Microscopy Promoter General Chemistry Chromatin Cell biology SAGA complex [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] 030104 developmental biology Saccharomycetales Trans-Activators lcsh:Q Protein Binding |
| Zdroj: | Nature Communications Nature Communications, Nature Publishing Group, 2017, 8 (1), ⟨10.1038/s41467-017-01564-7⟩ Nature Communications, Vol 8, Iss 1, Pp 1-7 (2017) |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-017-01564-7⟩ |
| Popis: | The transcription co-activator complex SAGA is recruited to gene promoters by sequence-specific transcriptional activators and by chromatin modifications to promote pre-initiation complex formation. The yeast Tra1 subunit is the major target of acidic activators such as Gal4, VP16, or Gcn4 but little is known about its structural organization. The 430 kDa Tra1 subunit and its human homolog the transformation/transcription domain-associated protein TRRAP are members of the phosphatidyl 3-kinase-related kinase (PIKK) family. Here, we present the cryo-EM structure of the entire SAGA complex where the major target of activator binding, the 430 kDa Tra1 protein, is resolved with an average resolution of 5.7 Å. The high content of alpha-helices in Tra1 enabled tracing of the majority of its main chain. Our results highlight the integration of Tra1 within the major epigenetic regulator SAGA. The transcription co-activator complex SAGA is recruited to promoters by transcriptional activators and promotes the formation of the pre-initiation complex. Here, the authors present the cryo-EM structure of the SAGA complex and resolve the major target of activator binding, the 430 kDa Tra1 protein. |
| Databáze: | OpenAIRE |
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