Cryo-EM structures of human RNA polymerase I
Copyright policy )Cryo-EM structures of human RNA polymerase I
Abstract 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.
Models, Molecular, Binding Sites, Transcription, Genetic, Protein Conformation, Cryoelectron Microscopy, Article, DNA-Binding Proteins, RNA Polymerase I, RNA, Ribosomal, Neoplasms, Humans, Protein Multimerization, Pol1 Transcription Initiation Complex Proteins, Protein Binding
Models, Molecular, Binding Sites, Transcription, Genetic, Protein Conformation, Cryoelectron Microscopy, Article, DNA-Binding Proteins, RNA Polymerase I, RNA, Ribosomal, Neoplasms, Humans, Protein Multimerization, Pol1 Transcription Initiation Complex Proteins, Protein Binding
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