Molecular Structures of Transcribing RNA Polymerase I.

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  • Additional Information
    • Source:
      Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-4164 (Electronic) Linking ISSN: 10972765 NLM ISO Abbreviation: Mol Cell Subsets: MEDLINE
    • Publication Information:
      Publication: Cambridge Ma : Cell Press
      Original Publication: Cambridge, Mass. : Cell Press, c1997-
    • Subject Terms:
      DNA/*chemistry ; Protein Subunits/*chemistry ; RNA/*chemistry ; RNA Polymerase I/*chemistry ; Saccharomyces cerevisiae/*chemistry ; Saccharomyces cerevisiae Proteins/*chemistry; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA/genetics ; DNA/metabolism ; Gene Expression ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Tertiary ; Protein Subunits/genetics ; Protein Subunits/isolation & purification ; Protein Subunits/metabolism ; RNA/genetics ; RNA/metabolism ; RNA Polymerase I/genetics ; RNA Polymerase I/isolation & purification ; RNA Polymerase I/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/isolation & purification ; Saccharomyces cerevisiae Proteins/metabolism
    • Abstract:
      RNA polymerase I (Pol I) is a 14-subunit enzyme that solely synthesizes pre-ribosomal RNA. Recently, the crystal structure of apo Pol I gave unprecedented insight into its molecular architecture. Here, we present three cryo-EM structures of elongating Pol I, two at 4.0 Å and one at 4.6 Å resolution, and a Pol I open complex at 3.8 Å resolution. Two modules in Pol I mediate the narrowing of the DNA-binding cleft by closing the clamp domain. The DNA is bound by the clamp head and by the protrusion domain, allowing visualization of the upstream and downstream DNA duplexes in one of the elongation complexes. During formation of the Pol I elongation complex, the bridge helix progressively folds, while the A12.2 C-terminal domain is displaced from the active site. Our results reveal the conformational changes associated with elongation complex formation and provide additional insight into the Pol I transcription cycle.
      (Copyright © 2016 The Author(s). Published by Elsevier Inc. All rights reserved.)
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    • Contributed Indexing:
      Keywords: Pol I; RNA polymerase I; cryoelectron microscopy; elongation complex; rDNA transcription; transcription
    • Accession Number:
      0 (Protein Subunits)
      0 (Recombinant Proteins)
      0 (Saccharomyces cerevisiae Proteins)
      63231-63-0 (RNA)
      9007-49-2 (DNA)
      EC 2.7.7.6 (RNA Polymerase I)
    • Publication Date:
      Date Created: 20161122 Date Completed: 20170905 Latest Revision: 20201209
    • Publication Date:
      20231215
    • Accession Number:
      PMC5179497
    • Accession Number:
      10.1016/j.molcel.2016.11.013
    • Accession Number:
      27867008