ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct
Summary: To understand the function of multisubunit complexes, it is of key importance to uncover the precise mechanisms that guide their assembly. Nascent proteins can find and bind their interaction partners during their translation, leading to co-translational assembly. Here, we demonstrate that...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-09-01
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| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124723011105 |
| _version_ | 1797689504857849856 |
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| author | Gizem Yayli Andrea Bernardini Paulina Karen Mendoza Sanchez Elisabeth Scheer Mylène Damilot Karim Essabri Bastien Morlet Luc Negroni Stéphane D. Vincent H.T. Marc Timmers László Tora |
| author_facet | Gizem Yayli Andrea Bernardini Paulina Karen Mendoza Sanchez Elisabeth Scheer Mylène Damilot Karim Essabri Bastien Morlet Luc Negroni Stéphane D. Vincent H.T. Marc Timmers László Tora |
| author_sort | Gizem Yayli |
| collection | DOAJ |
| description | Summary: To understand the function of multisubunit complexes, it is of key importance to uncover the precise mechanisms that guide their assembly. Nascent proteins can find and bind their interaction partners during their translation, leading to co-translational assembly. Here, we demonstrate that the core modules of ATAC (ADA-two-A-containing) and SAGA (Spt-Ada-Gcn5-acetyltransferase), two lysine acetyl transferase-containing transcription co-activator complexes, assemble co-translationally in the cytoplasm of mammalian cells. In addition, a SAGA complex containing all of its modules forms in the cytoplasm and acetylates non-histone proteins. In contrast, ATAC complex subunits cannot be detected in the cytoplasm of mammalian cells. However, an endogenous ATAC complex containing two functional modules forms and functions in the nucleus. Thus, the two related co-activators, ATAC and SAGA, assemble using co-translational pathways, but their subcellular localization, cytoplasmic abundance, and functions are distinct. |
| first_indexed | 2024-03-12T01:46:31Z |
| format | Article |
| id | doaj.art-7c3160e0e5134daeb9335018d23b6679 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-03-12T01:46:31Z |
| publishDate | 2023-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-7c3160e0e5134daeb9335018d23b66792023-09-09T04:55:01ZengElsevierCell Reports2211-12472023-09-01429113099ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinctGizem Yayli0Andrea Bernardini1Paulina Karen Mendoza Sanchez2Elisabeth Scheer3Mylène Damilot4Karim Essabri5Bastien Morlet6Luc Negroni7Stéphane D. Vincent8H.T. Marc Timmers9László Tora10Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceGerman Cancer Consortium (DKTK) Partner Site Freiburg, German Cancer Research Center (DKFZ), Freiburg, Germany; Department of Urology, Medical Center-University of Freiburg, Freiburg, GermanyInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, FranceGerman Cancer Consortium (DKTK) Partner Site Freiburg, German Cancer Research Center (DKFZ), Freiburg, Germany; Department of Urology, Medical Center-University of Freiburg, Freiburg, GermanyInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U1258, Illkirch, France; Université de Strasbourg, Illkirch, France; Corresponding authorSummary: To understand the function of multisubunit complexes, it is of key importance to uncover the precise mechanisms that guide their assembly. Nascent proteins can find and bind their interaction partners during their translation, leading to co-translational assembly. Here, we demonstrate that the core modules of ATAC (ADA-two-A-containing) and SAGA (Spt-Ada-Gcn5-acetyltransferase), two lysine acetyl transferase-containing transcription co-activator complexes, assemble co-translationally in the cytoplasm of mammalian cells. In addition, a SAGA complex containing all of its modules forms in the cytoplasm and acetylates non-histone proteins. In contrast, ATAC complex subunits cannot be detected in the cytoplasm of mammalian cells. However, an endogenous ATAC complex containing two functional modules forms and functions in the nucleus. Thus, the two related co-activators, ATAC and SAGA, assemble using co-translational pathways, but their subcellular localization, cytoplasmic abundance, and functions are distinct.http://www.sciencedirect.com/science/article/pii/S2211124723011105CP: Molecular biology |
| spellingShingle | Gizem Yayli Andrea Bernardini Paulina Karen Mendoza Sanchez Elisabeth Scheer Mylène Damilot Karim Essabri Bastien Morlet Luc Negroni Stéphane D. Vincent H.T. Marc Timmers László Tora ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct Cell Reports CP: Molecular biology |
| title | ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct |
| title_full | ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct |
| title_fullStr | ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct |
| title_full_unstemmed | ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct |
| title_short | ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct |
| title_sort | atac and saga co activator complexes utilize co translational assembly but their cellular localization properties and functions are distinct |
| topic | CP: Molecular biology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124723011105 |
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