Crystal structure of the 14-subunit RNA polymerase I
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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
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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