Crystal structure of the 14-subunit RNA polymerase I

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Crystal structure of the 14-subunit RNA polymerase I. / Fernández-Tornero, Carlos; Moreno-Morcillo, María; Rashid, Umar J; Taylor, Nicholas M I; Ruiz, Federico M; Gruene, Tim; Legrand, Pierre; Steuerwald, Ulrich; Müller, Christoph W.

In: Nature, Vol. 502, No. 7473, 2013, p. 644-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Fernández-Tornero, C, Moreno-Morcillo, M, Rashid, UJ, Taylor, NMI, Ruiz, FM, Gruene, T, Legrand, P, Steuerwald, U & Müller, CW 2013, 'Crystal structure of the 14-subunit RNA polymerase I', Nature, vol. 502, no. 7473, pp. 644-9. https://doi.org/10.1038/nature12636

APA

Fernández-Tornero, C., Moreno-Morcillo, M., Rashid, U. J., Taylor, N. M. I., Ruiz, F. M., Gruene, T., Legrand, P., Steuerwald, U., & Müller, C. W. (2013). Crystal structure of the 14-subunit RNA polymerase I. Nature, 502(7473), 644-9. https://doi.org/10.1038/nature12636

Vancouver

Fernández-Tornero C, Moreno-Morcillo M, Rashid UJ, Taylor NMI, Ruiz FM, Gruene T et al. Crystal structure of the 14-subunit RNA polymerase I. Nature. 2013;502(7473):644-9. https://doi.org/10.1038/nature12636

Author

Fernández-Tornero, Carlos ; Moreno-Morcillo, María ; Rashid, Umar J ; Taylor, Nicholas M I ; Ruiz, Federico M ; Gruene, Tim ; Legrand, Pierre ; Steuerwald, Ulrich ; Müller, Christoph W. / Crystal structure of the 14-subunit RNA polymerase I. In: Nature. 2013 ; Vol. 502, No. 7473. pp. 644-9.

Bibtex

@article{7123ac2ad8374a829be89a4a33b25433,
title = "Crystal structure of the 14-subunit RNA polymerase I",
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 {\AA} 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.",
keywords = "Catalytic Domain, Crystallography, X-Ray, DNA/chemistry, Models, Molecular, Peptide Chain Elongation, Translational, Protein Binding, Protein Conformation, Protein Multimerization, Protein Subunits/chemistry, RNA Polymerase I/chemistry, RNA Polymerase II/chemistry, RNA Polymerase III/chemistry, Saccharomyces cerevisiae/enzymology, Transcription, Genetic",
author = "Carlos Fern{\'a}ndez-Tornero and Mar{\'i}a Moreno-Morcillo and Rashid, {Umar J} and Taylor, {Nicholas M I} and Ruiz, {Federico M} and Tim Gruene and Pierre Legrand and Ulrich Steuerwald and M{\"u}ller, {Christoph W}",
year = "2013",
doi = "10.1038/nature12636",
language = "English",
volume = "502",
pages = "644--9",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",
number = "7473",

}

RIS

TY - JOUR

T1 - Crystal structure of the 14-subunit RNA polymerase I

AU - Fernández-Tornero, Carlos

AU - Moreno-Morcillo, María

AU - Rashid, Umar J

AU - Taylor, Nicholas M I

AU - Ruiz, Federico M

AU - Gruene, Tim

AU - Legrand, Pierre

AU - Steuerwald, Ulrich

AU - Müller, Christoph W

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - DNA/chemistry

KW - Models, Molecular

KW - Peptide Chain Elongation, Translational

KW - Protein Binding

KW - Protein Conformation

KW - Protein Multimerization

KW - Protein Subunits/chemistry

KW - RNA Polymerase I/chemistry

KW - RNA Polymerase II/chemistry

KW - RNA Polymerase III/chemistry

KW - Saccharomyces cerevisiae/enzymology

KW - Transcription, Genetic

U2 - 10.1038/nature12636

DO - 10.1038/nature12636

M3 - Journal article

C2 - 24153184

VL - 502

SP - 644

EP - 649

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7473

ER -

ID: 194520972