Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes
| العنوان: | Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes |
|---|---|
| المؤلفون: | Ikbal Cansu Baris, Sevil Zencir, Zeki Topcu, Muge Senarisoy, Melanie J. Dobson, Gizem Caliskan, Imre Boros, Ferhan Ayaydin |
| المساهمون: | Ege Üniversitesi |
| المصدر: | PLoS ONE PLoS ONE, Vol 12, Iss 12, p e0189193 (2017) |
| بيانات النشر: | Public Library of Science, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Molecular biology, transcription factor SAGA, lcsh:Medicine, Gene Expression, P300-CBP Transcription Factors, protein binding, yeast, immunoprecipitation, Biochemistry, Cell Fusion, Histones, 0302 clinical medicine, Transcription (biology), acyltransferase, Acetyltransferases/metabolism, Adaptor Proteins, Signal Transducing/metabolism, Histone Acetyltransferases/*metabolism, Humans, Protein Binding, Saccharomyces cerevisiae/*metabolism, Saccharomyces cerevisiae Proteins/*metabolism, Trans-Activators/*metabolism, Transcription Factors/metabolism, Transcriptional Activation, p300-CBP Transcription Factors/metabolism, p300-CBP Transcription Factors, lcsh:Science, transcription factor, cellular distribution, transcription initiation, Histone Acetyltransferases, Multidisciplinary, biology, histone acetyltransferase PCAF, TADA2A protein, human, Signal transducing adaptor protein, protein domain, protein function, reporter gene, 3. Good health, Cell biology, Precipitation Techniques, unclassified drug, Sgf29 protein, human, TADA2B protein, human, 030220 oncology & carcinogenesis, gene activity, protein protein interaction, p300-CBP-associated factor, Research Article, Cell Physiology, Apoptosis antagonizing transcription factor, Saccharomyces cerevisiae Proteins, Two-hybrid screening, DNA transcription, signal transducing adaptor protein, protein localization, Saccharomyces cerevisiae, DNA construction, DNA-binding protein, histone acetyltransferase, Article, genetic regulation, 03 medical and health sciences, Acetyltransferases, complex formation, DNA-binding proteins, Saccharomyces cerevisiae protein, Genetics, alteration deficiency in activation 2 protein, Gene Regulation, controlled study, human, cell protein, Protein Interactions, Transcription factor, protein expression, Adaptor Proteins, Signal Transducing, SAGA complex, S cerevisiae, nonhuman, human cell, lcsh:R, Biology and Life Sciences, Proteins, Histone acetyltransferase, Cell Biology, alteration deficiency in activation 3 protein, Co-Immunoprecipitation, Regulatory Proteins, Research and analysis methods, apoptosis antagonizing transcription factor, enzymes and coenzymes (carbohydrates), 030104 developmental biology, Molecular biology techniques, protein analysis, Plasmid Construction, biology.protein, Trans-Activators, lcsh:Q, mammal cell, histone acetyltransferase GCN5, metabolism, transactivator protein, Transcription Factors |
| الوصف: | WOS: 000417698200025 PubMed ID: 29232376 General Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA-and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes. Turkish Scientific and Technological Research Assembly [112T429]; Hungarian NRDIO [GINOP-2.3.2-15-2016-00020] This work was supported by the Turkish Scientific and Technological Research Assembly (112T429) (Dr. Sevil Zencir), and Hungarian NRDIO-GINOP-2.3.2-15-2016-00020 (Prof Imre M. Boros). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. |
| وصف الملف: | application/pdf; text |
| اللغة: | English |
| تدمد: | 0004-1769 2923-2376 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa09b7f075b8a6b906995e86eee21f0e https://hdl.handle.net/11499/8840 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....fa09b7f075b8a6b906995e86eee21f0e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00041769 29232376 |
|---|