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1. Atomic structure of the SAGA complex and it’s interaction with TBP

Author

Papai, Gabor, Frechard, Alexandre, Kolesnikova, Olga, Crucifix, Corinne, Schultz, Patrick, and Ben-Shem, Adam

Subjects
Genes, SGA, TBP, ARN messager, Transcription, Biology (General), QH301-705.5
Abstract

The transcription of eukaryotic protein genes is controlled by a plethora of proteins which act together in multi-component complexes to facilitate the DNA dependent RNA polymerase II (Pol II) enzyme to bind to the transcription start site and to generate messenger RNA from the gene’s coding sequence. The protein that guides the transcription machinery to the exact transcription start site is called TATA-box Binding Protein, or TBP. TBP is part of two large protein complexes involved in Pol II transcription, TFIID and SAGA. The two complexes share several subunits implicated in the interaction with TBP and contain proteins with structural elements highly homologous to nucleosomal histones. Despite the intensive study of transcription initiation, the mode of interaction of TBP with these complexes and its release upon DNA binding was elusive. In this study we demonstrate the quasi-atomic model of SAGA in complex with TBP. The structure reveals the intricate network of interactions that coordinate the different functional domains of SAGA and resolves a deformed octamer of histone-fold domains at the core of SAGA. This deformed octamer is precisely tuned to establish a peripheral site for TBP binding, where it is protected by steric hindrance against the binding of spurious DNA. Complementary biochemical analysis points to a mechanism for TBP delivery and release from SAGA that requires the general transcription factor TFIIA and whose efficiency correlates with the affinity of DNA to TBP.As the TBP binding machinery is highly similar in TFIID and SAGA, we demonstrated a universal mechanism of how TBP is delivered to gene promoters during transcription initiation.

Published
2021
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11. Structure of SAGA and mechanism of TBP deposition on gene promoters

Author

Papai, Gabor, Frechard, Alexandre, Kolesnikova, Olga, Crucifix, Corinne, Schultz, Patrick, and Ben-Shem, Adam

Subjects
Structure, Genetic aspects, Binding proteins -- Genetic aspects, Regulatory genes -- Structure, Promoters (Genetics) -- Genetic aspects, Genes -- Structure
Abstract

Author(s): Gabor Papai [sup.1] [sup.2] [sup.3] [sup.4] , Alexandre Frechard [sup.1] [sup.2] [sup.3] [sup.4] , Olga Kolesnikova [sup.1] [sup.2] [sup.3] [sup.4] , Corinne Crucifix [sup.1] [sup.2] [sup.3] [sup.4] , Patrick [...], SAGA (Spt-Ada-Gcn5-acetyltransferase) is a 19-subunit complex that stimulates transcription via two chromatin-modifying enzymatic modules and by delivering the TATA box binding protein (TBP) to nucleate the pre-initiation complex on DNA, a pivotal event in the expression of protein-encoding genes.sup.1. Here we present the structure of yeast SAGA with bound TBP. The core of the complex is resolved at 3.5 Å resolution (0.143 Fourier shell correlation). The structure reveals the intricate network of interactions that coordinate the different functional domains of SAGA and resolves an octamer of histone-fold domains at the core of SAGA. This deformed octamer deviates considerably from the symmetrical analogue in the nucleosome and is precisely tuned to establish a peripheral site for TBP, where steric hindrance represses binding of spurious DNA. Complementary biochemical analysis points to a mechanism for TBP delivery and release from SAGA that requires transcription factor IIA and whose efficiency correlates with the affinity of DNA to TBP. We provide the foundations for understanding the specific delivery of TBP to gene promoters and the multiple roles of SAGA in regulating gene expression. Structural studies on the yeast transcription coactivator complex SAGA (Spt-Ada-Gcn5-acetyltransferase) provide insights into the mechanism of initiation of regulated transcription by this multiprotein complex, which is conserved among eukaryotes.

Published
2020
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13. Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1

Author

Bednar, Jan, Garcia-Saez, Isabel, Boopathi, Ramachandran, Cutter, Amber R., Papai, Gabor, Reymer, Anna, Syed, Sajad H., Lone, Imtiaz Nisar, Tonchev, Ognyan, Crucifix, Corinne, Menoni, Hervé, Papin, Christophe, Skoufias, Dimitrios A., Kurumizaka, Hitoshi, Lavery, Richard, Hamiche, Ali, Hayes, Jeffrey J., Schultz, Patrick, Angelov, Dimitar, Petosa, Carlo, and Dimitrov, Stefan

Published
2017
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14. The Flexible Ends of CENP-A Nucleosome Are Required for Mitotic Fidelity

Author

Roulland, Yohan, Ouararhni, Khalid, Naidenov, Mladen, Ramos, Lorrie, Shuaib, Muhammad, Syed, Sajad Hussain, Lone, Imtiaz Nizar, Boopathi, Ramachandran, Fontaine, Emeline, Papai, Gabor, Tachiwana, Hiroaki, Gautier, Thierry, Skoufias, Dimitrios, Padmanabhan, Kiran, Bednar, Jan, Kurumizaka, Hitoshi, Schultz, Patrick, Angelov, Dimitar, Hamiche, Ali, and Dimitrov, Stefan

Published
2016
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20. The architecture of human general transcription factor TFIID core complex

Author

Bieniossek, Christoph, Papai, Gabor, Schaffitzel, Christiane, Garzoni, Frederic, Chaillet, Maxime, Scheer, Elisabeth, Papadopoulos, Petros, Tora, Laszlo, Schultz, Patrick, and Berger, Imre

Subjects
Structure, Observations, Transcription factors -- Structure -- Observations
Abstract

The initiation of gene transcription by RNA polymerase II is regulated by a plethora of proteins in human cells. The first general transcription factor to bind gene promoters is transcription [...]

Published
2013
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21. Architecture of the multi‐functional SAGA complex and the molecular mechanism of holding TBP

Author

Ben-Shem, Adam, Papai, Gabor, Schultz, Patrick, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), and Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV]Life Sciences [q-bio], genetic processes, information science, health occupations, cryo-EM, co-activators, TBP loading onto promoters, SAGA, macromolecular substances, transcription, environment and public health
Abstract

International audience; In eukaryotes, transcription of protein encoding genes is initiated by the controlled deposition of the TATA-box binding protein TBP onto gene promoters, followed by the ordered assembly of a pre-initiation complex. The SAGA co-activator is a 19-subunit complex that stimulates transcription by the action of two chromatin-modifying enzymatic modules, a transcription activator binding module, and by delivering TBP. Recent cryo electron microscopy structures of yeast SAGA with bound nucleosome or TBP reveal the architecture of the different functional domains of the co-activator. An octamer of histone fold domains is found at the core of SAGA. This octamer, which deviates considerably from the symmetrical analogue forming the nucleosome, establishes a peripheral site for TBP binding where steric hindrance represses interaction with spurious DNA. The structures point to a mechanism for TBP delivery and release from SAGA that requires TFIIA and whose efficiency correlates with the affinity of DNA to TBP. These results provide a structural basis for understanding specific TBP delivery onto gene promoters and the role played by SAGA in regulating gene expression. The properties of the TBP delivery machine harboured by SAGA are compared with the TBP loading device present in the TFIID complex and show multiple similitudes.

Published
2021
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22. TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiation

Author

Papai, Gabor, Tripathi, Manish K., Ruhlmann, Christine, Layer, Justin H., Weil, P. Anthony, and Schultz, Patrick

Subjects
Physiological aspects, Usage, Research, Binding sites (Biochemistry) -- Physiological aspects -- Research, Cryoelectron microscopy -- Usage, Transcription factors -- Physiological aspects -- Research, Messenger RNA -- Physiological aspects -- Research
Abstract

Three-dimensional electron microscopy has provided structural models for yeast TFIID (5,6) that bears close similarities with its human orthologue (7,8). TFIID can be divided into five modules (5,7), lobes A, [...], Transcription of eukaryotic messenger RNA (mRNA) encoding genes by RNA polymerase II (Pol II) is triggered by the binding of transactivating proteins to enhancer DNA, which stimulates the recruitment of general transcription factors (TFIIA, B, D, E, F, H) and Pol II on the cis-linked promoter, leading to pre-initiation complex formation and transcription (1). In TFIID-dependent activation pathways, this general transcription factor containing TATA-box-binding protein is first recruited on the promoter through interaction with activators (1-3) and cooperates with TFIIA to form a committed pre-initiation complex (4). However, neither the mechanisms by which activation signals are communicated between these factors nor the structural organization of the activated pre-initiation complex are known. Here we used cryo-electron microscopy to determine the architecture of nucleoprotein complexes composed of TFIID, TFIIA, the transcriptional activator Rap1 and yeast enhancer-promoter DNA. These structures revealed the mode of binding of Rap1 and TFIIA to TFIID, as well as a reorganization of TFIIA induced by its interaction with Rap1. We propose that this change in position increases the exposure of TATA-box-binding protein within TFIID, consequently enhancing its ability to interact with the promoter. A large Rap1-dependent DNA loop forms between the activator-binding site and the proximal promoter region. This loop is topologically locked by a TFIIA-Rap1 protein bridge that folds over the DNA. These results highlight the role of TFIIA in transcriptional activation, define a molecular mechanism for enhancer-promoter communication and provide structural insights into the pathways of intramolecular communication that convey transcription activation signals through the TFIID complex.

Published
2010
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30. H1–nucleosome interactions and their functional implications

Author

Sharma, Abhishek Bharadwaj, Van Dyck, Eric, Razvi, Syed Shoeb, Hasan, Mohammed Nihal, Hassan, Mohammed, Moselhy, Said Salama, Abualnaja, Khalid Omer, Kumosani, Taha Abduallah, Halwani, Majed, Asami, Tadao, Shukla, Manu, Soueidan, Lama, Noirclerc-Savoye, Marjolaine, Le Roy, Aline, Omran, Ziad, Zamzami, Mazin, Al-Malki, Abdulrahman Labeed, Choudhry, Hani, Andronov, Leonid, Michalon, Jonathan, Orlov, Igor, Vonesch, Jean-Luc, Klaholz, Bruno, Richert, Ludovic, Ashraf, Waseem, Alhosin, Mahmoud, Zaayter, Liliyana, Ahmad, Tanveer, Mély, Yves, Mousli, Marc, Garcia-Saez, Isabel, Cutter, Amber, Reymer, Anna, Syed, Sajad, Tonchev, Ognyan, Crucifix, Corinne, Lavery, Richard, Hayes, Jeffrey, Petosa, Carlo, Ibrahim, Abdulkhaleg, Gras, Stéphanie Le, VELT, Amandine, Jost, Bernard, Bronner, Christian, Fromental-Ramain, Catherine, Ramain, Philippe, Ors, Aysegul, Favier, Bertrand, Dalkara, Defne, Ozturk, Mehmet, Naidenov, Mladen, Ramos, Lorrie, Shuaib, Muhammad, Syed, Sajad Hussain, Lone, Imtiaz Nizar, Boopathi, Ramachandran, Fontaine, Emeline, Papai, Gabor, Tachiwana, Hiroaki, Gautier, Thierry, Skoufias, Dimitrios, Padmanabhan, Kiran, Kurumizaka, Hitoshi, Schultz, Patrick, Charles Richard, John Lalith, Shukla, Manu Shubhdarshan, Menoni, Hervé, Lone, Imtiaz Nisar, Roulland, Yohan, Ben Simon, Elsa, Kundu, Tapas, Angelov, Dimitar, Latrick, Chrysa, Marek, Martin, Ouararhni, Khalid, Papin, Christophe, Stoll, Isabelle, Ignatyeva, Maria, Obri, Arnaud, Ennifar, Eric, Romier, Christophe, Bednar, Jan, Hamiche, Ali, Dimitrov, Stefan, Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de Biologie Moléculaire de la Cellule (LBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Institut de biologie structurale (IBS - UMR 5075 ), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Louis Pasteur - Strasbourg I, Fonctions et dysfonctions épithéliales - UFC (EA 4267) (FDE), Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Laboratoire de Bioimagerie et Pathologies (UMR 7021), Université de Strasbourg (UNISTRA), Laboratoire de Biophotonique et Pharmacologie - UMR 7213 (LBP), Réseau nanophotonique et optique, Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Bioimagerie et Pathologies (LBP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institute for advanced biosciences, Uiversité de Lyon, 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), Laboratoire de biochimie théorique [Paris] (LBT (UPR_9080)), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Santé de la vigne et qualité du vin (SVQV), Université Louis Pasteur - Strasbourg I-Institut National de la Recherche Agronomique (INRA), Centre Léon Bérard [Lyon], Department of Medical Biology and Genetics, School of Medicine-Dokuz Eylul University, Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Institut cellule souche et cerveau (U846 Inserm - UCBL1), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris sciences et lettres (PSL), Synchronous programming for the trusted component-based engineering of embedded systems and mission-critical systems (ESPRESSO), Institut de Recherche en Informatique et Systèmes Aléatoires (IRISA), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Inria Rennes – Bretagne Atlantique, Institut National de Recherche en Informatique et en Automatique (Inria), Waseda University, Molecular Biology and Genetics Unit [Bangalore, India] (Transcription and Disease Laboratory), Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR)-Indian Institute of Science, Biologie moléculaire et cellulaire de la différenciation, Université Joseph Fourier - Grenoble 1 (UJF)-Institut Albert Bonniot-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de biologie moléculaire eucaryote (LBME), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Architecture et réactivité de l'ARN (ARN), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Spectrométrie Physique (LSP), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), INSERM U823, équipe 4 (Chromatine et Epigénétique), Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Réseau nanophotonique et optique, Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut National de la Recherche Agronomique (INRA)-Université de Strasbourg (UNISTRA), School of Medicine-Dokuz Eylül Üniversitesi = Dokuz Eylül University [Izmir] (DEÜ), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Louis Pasteur - Strasbourg I, Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Institut de Chimie du CNRS (INC), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Bioimagerie et Pathologie (LBP), Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), Institut National de la Recherche Agronomique (INRA)-Université Louis Pasteur - Strasbourg I, Centre National de la Recherche Scientifique (CNRS), Institut cellule souche et cerveau / Stem Cell and Brain Research Institute (SBRI), PSL Research University (PSL), Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC), and Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Histone-modifying enzymes, Molecular Sequence Data, Biophysics, Biochemistry, Histones, 03 medical and health sciences, Structural Biology, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Genetics, Animals, Humans, Nucleosome, Histone code, Amino Acid Sequence, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Chromatin Fiber, 030102 biochemistry & molecular biology, biology, Chromatin Assembly and Disassembly, Linker DNA, Nucleosomes, Chromatin, 030104 developmental biology, Histone, Gene Expression Regulation, Chromatosome, biology.protein
Abstract

Linker histones are three domain proteins and consist of a structured (globular) domain, flanked by two likely non-structured NH2- and COOH-termini. The binding of the linker histones to the nucleosome was characterized by different methods in solution. Apparently, the globular domain interacts with the linker DNA and the nucleosome dyad, while the binding of the large and rich in lysines COOH-terminus results in "closing" the linker DNA of the nucleosome and the formation of the "stem" structure. What is the mode of binding of the linker histones within the chromatin fiber remains still elusive. Nonetheless, it is clear that linker histones are essential for both the assembly and maintenance of the condensed chromatin fiber. Interestingly, linker histones are post-translationally modified and how this affects both their binding to chromatin and functions is now beginning to emerge. In addition, linker histones are highly mobile in vivo, but not in vitro. No explanation of this finding is reported for the moment. The higher mobility of the linker histones should, however, have strong impact on their function. Linker histones plays an important role in gene expression regulation and other chromatin related process and their function is predominantly regulated by their posttranslational modifications. However, the detailed mechanism how the linker histones do function remains still not well understood despite numerous efforts. Here we will summarize and analyze the data on the linker histone binding to the nucleosome and the chromatin fiber and will discuss its functional consequences.

Published
2016
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32. A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion

Author

Botte, Mathieu, primary, Zaccai, Nathan R., additional, Nijeholt, Jelger Lycklama à., additional, Martin, Remy, additional, Knoops, Kèvin, additional, Papai, Gabor, additional, Zou, Juan, additional, Deniaud, Aurélien, additional, Karuppasamy, Manikandan, additional, Jiang, Qiyang, additional, Roy, Abhishek Singha, additional, Schulten, Klaus, additional, Schultz, Patrick, additional, Rappsilber, Juri, additional, Zaccai, Giuseppe, additional, Berger, Imre, additional, Collinson, Ian, additional, and Schaffitzel, Christiane, additional

Published
2016
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34. Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules

Author

Trowitzsch, Simon, primary, Viola, Cristina, additional, Scheer, Elisabeth, additional, Conic, Sascha, additional, Chavant, Virginie, additional, Fournier, Marjorie, additional, Papai, Gabor, additional, Ebong, Ima-Obong, additional, Schaffitzel, Christiane, additional, Zou, Juan, additional, Haffke, Matthias, additional, Rappsilber, Juri, additional, Robinson, Carol V., additional, Schultz, Patrick, additional, Tora, Laszlo, additional, and Berger, Imre, additional

Published
2015
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39. [Transcriptional regulation by the coactivator TFIID].

Author

Papai G and Schultz P

Subjects
Animals, DNA metabolism, Humans, Models, Molecular, Protein Conformation, Protein Interaction Mapping, Protein Subunits, TATA Box, TATA-Binding Protein Associated Factors metabolism, TATA-Box Binding Protein metabolism, Transcription Factor TFIIA metabolism, Transcription Factor TFIID chemistry, Transcription Factor TFIID physiology, Transcription, Genetic physiology
Published
2010
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