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TitleCryo-EM structures of human RNA polymerase I.
Journal, issue, pagesNat Struct Mol Biol, Vol. 28, Issue 12, Page 997-991008, Year 2021
Publish dateDec 9, 2021
AuthorsAgata D Misiaszek / Mathias Girbig / Helga Grötsch / Florence Baudin / Brice Murciano / Aleix Lafita / Christoph W Müller /
PubMed AbstractRNA polymerase I (Pol I) specifically synthesizes ribosomal RNA. Pol I upregulation is linked to cancer, while mutations in the Pol I machinery lead to developmental disorders. Here we report the ...RNA polymerase I (Pol I) specifically synthesizes ribosomal RNA. Pol I upregulation is linked to cancer, while mutations in the Pol I machinery lead to developmental disorders. Here we report the cryo-EM structure of elongating human Pol I at 2.7 Å resolution. In the exit tunnel, we observe a double-stranded RNA helix that may support Pol I processivity. Our structure confirms that human Pol I consists of 13 subunits with only one subunit forming the Pol I stalk. Additionally, the structure of human Pol I in complex with the initiation factor RRN3 at 3.1 Å resolution reveals stalk flipping upon RRN3 binding. We also observe an inactivated state of human Pol I bound to an open DNA scaffold at 3.3 Å resolution. Lastly, the high-resolution structure of human Pol I allows mapping of disease-related mutations that can aid understanding of disease etiology.
External linksNat Struct Mol Biol / PubMed:34887565 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.3 Å
Structure data

12795

7ob9

EMDB-12795, PDB-7ob9:
Cryo-EM structure of human RNA Polymerase I in elongation state
Method: EM (single particle) / Resolution: 2.7 Å

12796

7oba

EMDB-12796, PDB-7oba:
Cryo-EM structure of human RNA Polymerase I in complex with RRN3
Method: EM (single particle) / Resolution: 3.1 Å

12797

7obb

EMDB-12797, PDB-7obb:
Cryo-EM structure of human RNA Polymerase I Open Complex
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / RNA polymerase I / human / rRNA transcription / DNA-dependent RNA polymerase / elongation state / pre-initiation / RRN3 / Open Complex

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