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Crystal structure of the 14-subunit RNA polymerase I

Author

Listed:
  • Carlos Fernández-Tornero

    (Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain)

  • María Moreno-Morcillo

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

  • Umar J. Rashid

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

  • Nicholas M. I. Taylor

    (Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain)

  • Federico M. Ruiz

    (Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain)

  • Tim Gruene

    (Georg-August-University, Tammannstraße 4, 37077 Göttingen, Germany)

  • Pierre Legrand

    (SOLEIL Synchrotron, L’Orme des Merisiers Saint Aubin, 91192 Gif-sur-Yvette, France)

  • Ulrich Steuerwald

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany
    Present address: Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany.)

  • Christoph W. Müller

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

Abstract

Protein biosynthesis depends on the availability of ribosomes, which in turn relies on ribosomal RNA production. In eukaryotes, this process is carried out by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a major determinant of cell growth. Here we present the crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution. The Pol I structure shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An extended loop mimics the DNA backbone in the cleft and may be involved in regulating Pol I transcription. Subunit A12.2 extends from the A190 jaw to the active site and inserts a transcription elongation factor TFIIS-like zinc ribbon into the nucleotide triphosphate entry pore, providing insight into the role of A12.2 in RNA cleavage and Pol I insensitivity to α-amanitin. The A49–A34.5 heterodimer embraces subunit A135 through extended arms, thereby contacting and potentially regulating subunit A12.2.

Suggested Citation

  • Carlos Fernández-Tornero & María Moreno-Morcillo & Umar J. Rashid & Nicholas M. I. Taylor & Federico M. Ruiz & Tim Gruene & Pierre Legrand & Ulrich Steuerwald & Christoph W. Müller, 2013. "Crystal structure of the 14-subunit RNA polymerase I," Nature, Nature, vol. 502(7473), pages 644-649, October.
    • Handle: RePEc:nat:nature:v:502:y:2013:i:7473:d:10.1038_nature12636
    DOI: 10.1038/nature12636
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    Cited by:

    1. Maxime Duval & Carlo Yague-Sanz & Tomasz W. Turowski & Elisabeth Petfalski & David Tollervey & François Bachand, 2023. "The conserved RNA-binding protein Seb1 promotes cotranscriptional ribosomal RNA processing by controlling RNA polymerase I progression," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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