Evolution, Structure and Assembly of Basal Transcription Factor II D
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Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-Like Mouse Models: Tracking the Role of the Hairless Gene
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 5-2006 Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-like Mouse Models: Tracking the Role of the Hairless Gene Yutao Liu University of Tennessee - Knoxville Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Life Sciences Commons Recommended Citation Liu, Yutao, "Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino- like Mouse Models: Tracking the Role of the Hairless Gene. " PhD diss., University of Tennessee, 2006. https://trace.tennessee.edu/utk_graddiss/1824 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Yutao Liu entitled "Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-like Mouse Models: Tracking the Role of the Hairless Gene." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Life Sciences. Brynn H. Voy, Major Professor We have read this dissertation and recommend its acceptance: Naima Moustaid-Moussa, Yisong Wang, Rogert Hettich Accepted for the Council: Carolyn R. -
A Versatile Group of Transcriptional Regulators in Archaea
Extremophiles (2014) 18:925–936 DOI 10.1007/s00792-014-0677-2 SPECIAL ISSUE: REVIEW 10th International Congress on Extremophiles The TrmB family: a versatile group of transcriptional regulators in Archaea Antonia Gindner • Winfried Hausner • Michael Thomm Received: 14 March 2014 / Accepted: 10 July 2014 / Published online: 13 August 2014 Ó The Author(s) 2014. This article is published with open access at Springerlink.com Abstract Microbes are organisms which are well adapted and Wheelis in 1990 (Woese et al. 1990). This was con- to their habitat. Their survival depends on the regulation of firmed later by studies of the Archaeal biochemistry and gene expression levels in response to environmental signals. molecular biology. What distinguishes Archaea from the The most important step in regulation of gene expression other two domains is the fact that they possess both bacterial takes place at the transcriptional level. This regulation is and eukaryal properties. On the one hand, they have tran- intriguing in Archaea because the eu-karyotic-like tran- scription, translation and DNA replication machineries scription apparatus is modulated by bacterial-like tran- which are similar to those of eukaryotic organisms (Keeling scription regulators. The transcriptional regulator of mal and Doolittle 1995; Langer et al. 1995; Dennis 1997; Gra- operon (TrmB) family is well known as a very large group of bowski and Kelman 2003). On the other hand, many genes regulators in Archaea with more than 250 members to date. involved in metabolic processes are more similar to those One special feature of these regulators is that some of them encoded in bacterial genomes (Koonin et al. -
Evolution of Two Modes of Intrinsic RNA Polymerase Transcript Cleavage
Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München Evolution of two modes of intrinsic RNA polymerase transcript cleavage Wenjie Ruan aus Anhui, P.R.China 2011 Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München Evolution of two modes of intrinsic RNA polymerase transcript cleavage Wenjie Ruan aus Anhui, P.R.China 2011 Erklärung II Erklärung Diese Dissertation wurde im Sinne von §13 Abs. 3 der Promotionsordnung vom 29. Januar 1998 (in der Fassung der vierten Änderungssatzung vom 26. November 2004) von Herrn Prof. Dr. Patrick Cramer betreut. Ehrenwörtliche Versicherung Diese Dissertation wurde selbständig und ohne unerlaubte Hilfe erarbeitet. München, den 06. April 2011 ______________________________ Wenjie Ruan Dissertation eingereicht am 07. April 2011 1. Gutachter: Prof. Dr. Patrick Cramer 2. Gutachter: Prof. Dr. Dietmar Martin Mündliche Prüfung am 11.Mai 2011 Acknowledgements III Acknowledgements Five years ago, on the beautiful fall of 2006, when I first set foot on this land, colorful leaves, blue sky, smiling and courteous people, were the first impressions Deutschland gave me. This was my first time coming abroad, touching a completely different world and culture. During the last years, I harvested a lot, both on academic life, and on mentality, grown up to be a strong person. The long journey would not have been possible without the help of many people. I wish to give them my sincere thanks here. Prof. Patrick Cramer, you are the first and most important person I want to thank. As a foreign student, huge differences on culture and language once gave me a lot of pressure. -
Taenia Solium TAF6 and TAF9 Binds to a Putative Downstream Promoter Element
bioRxiv preprint doi: https://doi.org/10.1101/106997; this version posted February 8, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Taenia solium TAF6 and TAF9 binds to a putative Downstream Promoter Element present in TsTBP1 gene core promoter. Oscar Rodríguez-Lima1, #a, Ponciano García-Gutierrez2, Lucía Jimenez1, Angel Zarain-Herzberg3, Roberto Lazarini4 and Abraham Landa1*. 1Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México. Ciudad de México, México. 2Departamento de Química, Universidad Autónoma Metropolitana–Iztapalapa. Ciudad de México, México. 3Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México. Ciudad de México, México. 4Departamento de Biología Experimental, Universidad Autónoma Metropolitana– Iztapalapa. Ciudad de México, México. #a Current address: Center for Integrative Genomics, Lausanne University, Lausanne, Switzerland. *Corresponding author: Abraham Landa, Ph.D. Universidad Nacional Autónoma de México. Departamento de Microbiología y Parasitología, Facultad de Medicina Edificio A 2do piso. Ciudad Universitaria. CDMX 04510, México Phone: (52 55) 56-23-23-57, Fax: (52 55) 56-23-23-82, Email: [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/106997; this version posted February 8, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. -
Molecular Structure of Promoter-Bound Yeast TFIID
ARTICLE DOI: 10.1038/s41467-018-07096-y OPEN Molecular structure of promoter-bound yeast TFIID Olga Kolesnikova 1,2,3,4, Adam Ben-Shem1,2,3,4, Jie Luo5, Jeff Ranish 5, Patrick Schultz 1,2,3,4 & Gabor Papai 1,2,3,4 Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBP- associate factors (Tafs) providing regulatory and chromatin binding functions. Here we present the cryo-electron microscopy structure of promoter-bound yeast TFIID at a resolu- 1234567890():,; tion better than 5 Å, except for a flexible domain. We position the crystal structures of several subunits and, in combination with cross-linking studies, describe the quaternary organization of TFIID. The compact tri lobed architecture is stabilized by a topologically closed Taf5-Taf6 tetramer. We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a histone fold domain in the Twin lobe. 1 Department of Integrated Structural Biology, Equipe labellisée Ligue Contre le Cancer, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch 67404, France. 2 Centre National de la Recherche Scientifique, UMR7104, 67404 Illkirch, France. 3 Institut National de la Santé et de la Recherche Médicale, U1258, 67404 Illkirch, France. 4 Université de Strasbourg, Illkirch 67404, France. 5 Institute for Systems Biology, Seattle, WA 98109, USA. These authors contributed equally: Olga Kolesnikova, Adam Ben-Shem. Correspondence and requests for materials should be addressed to P.S. (email: [email protected]) or to G.P. -
Characterization of Regulatory Sequences in Alternative Promoters of Hypermethylated Genes Associated with Tumor Resistance to Cisplatin
408 MOLECULAR AND CLINICAL ONCOLOGY 3: 408-414, 2015 Characterization of regulatory sequences in alternative promoters of hypermethylated genes associated with tumor resistance to cisplatin MOHAMMED A. IBRAHIM-ALOBAIDE1, ABDELSALAM G. ABDELSALAM2,3, HYTHAM ALOBYDI4, KAKIL IBRAHIM RASUL5, RUIWEN ZHANG6 and KALKUNTE S. SRIVENUGOPAL1 1Department of Biomedical Sciences and Cancer Biology Research Center, School of Pharmacy, Texas Tech University Health Sciences Center, Amarillo, TX 79106, USA; 2Department of Mathematics, Statistics and Physics, College of Arts and Sciences, Qatar University, Doha, Qatar; 3Department of Statistics, Faculty of Economics and Political Sciences, Cairo University, Giza 12613, Egypt; 4Biomedica, LLC, Sterling Heights, MI 48310, USA; 5Weill Cornell Medical College and Hamad Medical Corporation, Doha, Qatar; 6Department of Pharmaceutical Sciences and Cancer Biology Research Center, School of Pharmacy, Texas Tech University Health Sciences Center, Amarillo, TX 79106, USA Received October 7, 2014; Accepted October 23, 2014 DOI: 10.3892/mco.2014.468 Abstract. The development of cisplatin resistance in human TATA-8 and were found in all the promoters. B recognition cancers is controlled by multiple genes and leads to therapeutic element (BRE) sequences were present only in alternative failure. Hypermethylation of specific gene promoters is a key promoters harboring CGIs, but CCAAT and TAACC were event in clinical resistance to cisplatin. Although the usage of found in both types of alternative promoters, whereas down- multiple promoters is frequent in the transcription of human stream promoter element sequences were significantly less genes, the role of alternative promoters and their regulatory frequent. Therefore, it was hypothesized that BRE and CGI sequences have not yet been investigated in cisplatin resistance sequences co-localized in alternative promoters of cisplatin genes. -
Supplementary Methods
Weake2009 Supplemental Methods 1 Supplemental methods Preparation of soluble nuclear extracts, affinity purification and MudPIT analysis Nuclear extracts were prepared and affinity purifications conducted from 4 L of S2 cells grown to a density of 1 x 107cells/mL in Hyclone SFX media with low/no copper induction. Cells were collected by centrifugation at 5000 rpm 15 min 4ºC and washed in Wash Buffer (10 mM HEPEs [Na+], pH 7.5; 140 mM NaCl). Cells were resuspended in + 40mL of Buffer I (15 mM HEPEs [Na ] pH 7.5; 10 mM KCl, 5 mM MgCl2; 0.1 mM EDTA; 0.5 mM EGTA; 350 mM sucrose; supplemented with 20 g/mL leupeptin, 20 g/mL pepstatin and 100 M PMSF) and disrupted by 40 strokes in a Dounce homogenizer with the loose pestle. Nuclei were collected by centrifugation at 10,400 x g 15 min 4ºC and washed once with 40 mL of Buffer I. The soluble nuclear fraction was isolated by resuspending nuclei in 20 mL of Extraction Buffer (20 mM HEPEs [Na+], pH 7.5; 10% glycerol; 350 mM NaCl; 1 mM MgCl2; 0.1% TritonX-100; supplemented with 20 g/mL leupeptin, 20 g/mL pepstatin and 100 M PMSF) for 1 h 4ºC with rotation, followed by centrifugation to pellet the insoluble chromatin fraction at 18,000 x g 10 min 4ºC. The soluble nuclear extract was cleared by centrifugation at 40,000 rpm 1.5 h 4ºC. Nuclear extracts were diluted to a final salt concentration of 300 mM NaCl and incubated with FLAG-agarose. -
Molecular Mechanisms of Ribosomal Protein Gene Coregulation
Downloaded from genesdev.cshlp.org on October 3, 2021 - Published by Cold Spring Harbor Laboratory Press Molecular mechanisms of ribosomal protein gene coregulation Rohit Reja, Vinesh Vinayachandran, Sujana Ghosh, and B. Franklin Pugh Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, Pennsylvania 16802, USA The 137 ribosomal protein genes (RPGs) of Saccharomyces provide a model for gene coregulation. We examined the positional and functional organization of their regulators (Rap1 [repressor activator protein 1], Fhl1, Ifh1, Sfp1, and Hmo1), the transcription machinery (TFIIB, TFIID, and RNA polymerase II), and chromatin at near-base-pair res- olution using ChIP-exo, as RPGs are coordinately reprogrammed. Where Hmo1 is enriched, Fhl1, Ifh1, Sfp1, and Hmo1 cross-linked broadly to promoter DNA in an RPG-specific manner and demarcated by general minor groove widening. Importantly, Hmo1 extended 20–50 base pairs (bp) downstream from Fhl1. Upon RPG repression, Fhl1 remained in place. Hmo1 dissociated, which was coupled to an upstream shift of the +1 nucleosome, as reflected by the Hmo1 extension and core promoter region. Fhl1 and Hmo1 may create two regulatable and positionally distinct barriers, against which chromatin remodelers position the +1 nucleosome into either an activating or a repressive state. Consistent with in vitro studies, we found that specific TFIID subunits, in addition to cross-linking at the core promoter, made precise cross-links at Rap1 sites, which we interpret to reflect native Rap1–TFIID interactions. Our findings suggest how sequence-specific DNA binding regulates nucleosome positioning and transcription complex assembly >300 bp away and how coregulation coevolved with coding sequences. -
TAF10 Complex Provides Evidence for Nuclear Holo&Ndash;TFIID Assembly from Preform
ARTICLE Received 13 Aug 2014 | Accepted 2 Dec 2014 | Published 14 Jan 2015 DOI: 10.1038/ncomms7011 OPEN Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules Simon Trowitzsch1,2, Cristina Viola1,2, Elisabeth Scheer3, Sascha Conic3, Virginie Chavant4, Marjorie Fournier3, Gabor Papai5, Ima-Obong Ebong6, Christiane Schaffitzel1,2, Juan Zou7, Matthias Haffke1,2, Juri Rappsilber7,8, Carol V. Robinson6, Patrick Schultz5, Laszlo Tora3 & Imre Berger1,2,9 General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID—a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)— assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8–TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core–TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo–TFIID, regulated by nuclear import of preformed cytoplasmic submodules. 1 European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, 38042 Grenoble, France. 2 Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble, France. 3 Cellular Signaling and Nuclear Dynamics Program, Institut de Ge´ne´tique et de Biologie Mole´culaire et Cellulaire, UMR 7104, INSERM U964, 1 rue Laurent Fries, 67404 Illkirch, France. -
MAF1 Represses CDKN1A Through a Pol III-Dependent Mechanism Yu-Ling Lee, Yuan-Ching Li, Chia-Hsin Su, Chun-Hui Chiao, I-Hsuan Lin, Ming-Ta Hsu*
RESEARCH ARTICLE elifesciences.org MAF1 represses CDKN1A through a Pol III-dependent mechanism Yu-Ling Lee, Yuan-Ching Li, Chia-Hsin Su, Chun-Hui Chiao, I-Hsuan Lin, Ming-Ta Hsu* Institute of Biochemistry and Molecular Biology, School of Life Science, National Yang-Ming University, Taipei, Taiwan Abstract MAF1 represses Pol III-mediated transcription by interfering with TFIIIB and Pol III. Herein, we found that MAF1 knockdown induced CDKN1A transcription and chromatin looping concurrently with Pol III recruitment. Simultaneous knockdown of MAF1 with Pol III or BRF1 (subunit of TFIIIB) diminished the activation and looping effect, which indicates that recruiting Pol III was required for activation of Pol II-mediated transcription and chromatin looping. Chromatin- immunoprecipitation analysis after MAF1 knockdown indicated enhanced binding of Pol III and BRF1, as well as of CFP1, p300, and PCAF, which are factors that mediate active histone marks, along with the binding of TATA binding protein (TBP) and POLR2E to the CDKN1A promoter. Simultaneous knockdown with Pol III abolished these regulatory events. Similar results were obtained for GDF15. Our results reveal a novel mechanism by which MAF1 and Pol III regulate the activity of a protein- coding gene transcribed by Pol II. DOI: 10.7554/eLife.06283.001 Introduction Transcription by RNA polymerase III (Pol III) is regulated by MAF1, which is a highly conserved protein in eukaryotes (Pluta et al., 2001; Reina et al., 2006). MAF1 represses Pol III transcription through *For correspondence: mth@ym. association with BRF1, a subunit of initiation factor TFIIIB, which prevents attachment of TFIIIB onto edu.tw DNA. -
Characterization of Labelled Regulatory Elements in Embryonic Stem Cells and Macrophages Using Quantitative and Qualitative Methods
THESIS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY (PHD) Characterization of labelled regulatory elements in embryonic stem cells and macrophages using quantitative and qualitative methods by Attila Horváth UNIVERSITY OF DEBRECEN DOCTORAL SCHOOL OF MOLECULAR CELL AND IMMUNE BIOLOGY DEBRECEN, 2019 THESIS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY (PHD) Characterization of labelled regulatory elements in embryonic stem cells and macrophages using quantitative and qualitative methods by Attila Horváth Supervisor: Prof. Dr. László Nagy Co-Supervisor: Dr. Benedek Nagy UNIVERSITY OF DEBRECEN DOCTORAL SCHOOL OF MOLECULAR CELL AND IMMUNE BIOLOGY DEBRECEN, 2019 2 TABLE OF CONTENT 1. ABBREVIATIONS ..................................................................................................................................... 6 2. INTRODUCTION .................................................................................................................................... 10 Transcription regulation in Eukaryotes ......................................................................................................... 10 The concept of enhancer ............................................................................................................................. 12 Identification of enhancer regions................................................................................................................ 13 Histone modifications ................................................................................................................................. -
Repression of RNA Polymerase by the Archaeo-Viral Regulator
Edinburgh Research Explorer Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP Citation for published version: Sheppard, C, Blombach, F, Belsom, A, Schulz, S, Daviter, T, Smollett, K, Mahieu, E, Erdmann, S, Tinnefeld, P, Garrett, R, Grohmann, D, Rappsilber, J & Werner, F 2016, 'Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP', Nature Communications, vol. 7, 13595. https://doi.org/10.1038/ncomms13595 Digital Object Identifier (DOI): 10.1038/ncomms13595 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Nature Communications General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 06. Oct. 2021 ARTICLE Received 4 May 2016 | Accepted 18 Oct 2016 | Published 24 Nov 2016 DOI: 10.1038/ncomms13595 OPEN Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP Carol Sheppard1, Fabian Blombach1, Adam Belsom2, Sarah Schulz3, Tina Daviter1, Katherine Smollett1, Emilie Mahieu1, Susanne Erdmann4, Philip Tinnefeld3, Roger Garrett4, Dina Grohmann3,w, Juri Rappsilber2,5 & Finn Werner1 Little is known about how archaeal viruses perturb the transcription machinery of their hosts.