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      RNA polymerase I activation and hibernation: unique mechanisms for unique genes

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          ABSTRACT

          In yeast, transcription of ribosomal DNA (rDNA) by RNA polymerase I (Pol I) is regulated by unique mechanisms acting at the level of the enzyme. Under stress situations such as starvation, Pol I hibernates through dimerization. When growth conditions are restored, dimer disassembly and Rrn3 binding drive enzyme activation and subsequent recruitment to rDNA.

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          Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.

          P. Cramer, D. Bushnell, R D Kornberg (2001)
          Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.
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            A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II.

            Roger D. Kornberg, Yingqiu Li, S Bjorklund … (1994)
            A mediator was isolated from yeast that enabled a response to the activator proteins GAL4-VP16 and GCN4 in a transcription system reconstituted with essentially homogeneous basal factors and RNA polymerase II. The mediator comprised some 20 polypeptides, including the three subunits of TFIIF and other polypeptides cross-reactive with antisera against GAL11, SUG1, SRB2, SRB4, SRB5, and SRB6 proteins. Mediator not only enabled activated transcription but also conferred 8-fold greater activity in basal transcription and 12-fold greater efficiency of phosphorylation of RNA polymerase II by the TFIIH-associated C-terminal repeat domain (CTD) kinase, indicative of mediator-CTD interaction. A holoenzyme form of RNA polymerase II was independently isolated that supported a response to activator proteins with purified basal factors. The holoenzyme proved to consist of mediator associated with core 12-subunit RNA polymerase II.
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              Dysregulation of the basal RNA polymerase transcription apparatus in cancer.

              B. Pearson, Ross D. Hannan, M Bywater … (2013)
              Mutations that directly affect transcription by RNA polymerases rank among the most central mediators of malignant transformation, but the frequency of new anticancer drugs that selectively target defective transcription apparatus entering the clinic has been limited. This is because targeting the large protein-protein and protein-DNA interfaces that control both generic and selective aspects of RNA polymerase transcription has proved extremely difficult. However, recent technological advances have led to a 'quantum leap' in our comprehension of the structure and function of the core RNA polymerase components, how they are dysregulated in a broad range of cancers and how they may be targeted for 'transcription therapy'.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Transcription
                Journal ID (iso-abbrev): Transcription
                Journal ID (publisher-id): KTRN
                Journal ID (publisher-id): ktrn20
                Title: Transcription
                Publisher: Taylor & Francis
                ISSN (Print): 2154-1264
                ISSN (Electronic): 2154-1272
                Publication date Collection: 2018
                Publication date (Electronic): 26 January 2018
                Publication date PMC-release: 26 January 2018
                Volume: 9
                Issue: 4
                Pages: 248-254
                Affiliations
                Centro de Investigaciones Biológicas – CSIC , Ramiro de Maeztu 9, 28040 Madrid, Spain
                Author notes
                Carlos Fernández-Tornero cftornero@ 123456cib.csic.es , Centro de Investigaciones Biológicas – CSIC , Ramiro de Maeztu 9, 28040 Madrid, Spain.
                Author information
                http://orcid.org/0000-0001-5097-731X
                Article
                Publisher ID: 1416267
                DOI: 10.1080/21541264.2017.1416267
                PMC ID: 6104688
                PubMed ID: 29372670
                SO-VID: 0c20118c-35f0-4dcd-8799-3be4f06ef70f
                Copyright © © 2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License ( http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

                History
                Date received : 6 November 2017
                Date revision received : 1 December 2017
                Date accepted : 4 December 2017
                Page count
                Figures: 2, Tables: 0, References: 41, Pages: 7
                Funding
                Funded by: Spanish Ministry of Economy and Competitiveness (MINECO) 10.13039/501100003329
                Award ID: BFU2013-48374-P
                Funded by: Ramón Areces Foundation 10.13039/100008054
                This work was supported by the Spanish Ministry of Economy and Competitiveness (MINECO) under Grant BFU2013-48374-P and by the Ramón Areces Foundation.
                Categories
                Subject: Point-of-View

                ScienceOpen disciplines: Molecular biology
                Keywords: ribosomal dna,rna polymerase i,transcriptional regulation,conformational state,enzyme activation,enzyme hibernation,cell growth
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: ribosomal dna, rna polymerase i, transcriptional regulation, conformational state, enzyme activation, enzyme hibernation, cell growth

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