DNA-directed RNA polymerase II subunit RPB1 / DNA-directed RNA polymerase II subunit RPB2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / Transcription elongation factor SPT5 / DNA-directed RNA polymerase II subunit RPB9 ...DNA-directed RNA polymerase II subunit RPB1 / DNA-directed RNA polymerase II subunit RPB2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / Transcription elongation factor SPT5 / DNA-directed RNA polymerase II subunit RPB9 / DNA-directed RNA polymerase II subunit RPB7 / DNA-directed RNA polymerase II subunit RPB11 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / Decapping nuclease RAI1 / 5'-3' exoribonuclease 2 Similarity search - Component
Journal: Nature / Year: 2024 Title: Structural basis of exoribonuclease-mediated mRNA transcription termination. Authors: Yuan Zeng / Hong-Wei Zhang / Xiao-Xian Wu / Yu Zhang / Abstract: Efficient termination is required for robust gene transcription. Eukaryotic organisms use a conserved exoribonuclease-mediated mechanism to terminate the mRNA transcription by RNA polymerase II ...Efficient termination is required for robust gene transcription. Eukaryotic organisms use a conserved exoribonuclease-mediated mechanism to terminate the mRNA transcription by RNA polymerase II (Pol II). Here we report two cryogenic electron microscopy structures of Saccharomyces cerevisiae Pol II pre-termination transcription complexes bound to the 5'-to-3' exoribonuclease Rat1 and its partner Rai1. Our structures show that Rat1 displaces the elongation factor Spt5 to dock at the Pol II stalk domain. Rat1 shields the RNA exit channel of Pol II, guides the nascent RNA towards its active centre and stacks three nucleotides at the 5' terminus of the nascent RNA. The structures further show that Rat1 rotates towards Pol II as it shortens RNA. Our results provide the structural mechanism for the Rat1-mediated termination of mRNA transcription by Pol II in yeast and the exoribonuclease-mediated termination of mRNA transcription in other eukaryotes.
UniProtKB: DNA-directed RNA polymerase II subunit RPB1
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Macromolecule #2: DNA-directed RNA polymerase II subunit RPB2
Macromolecule
Name: DNA-directed RNA polymerase II subunit RPB2 / type: protein_or_peptide / ID: 2 Details: Residues (1225B-1259B) are an affinity tag(containing a TEV-6xHis-3xFlag tag) we modified in the genome of target strain for convenient protein purification. Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC4
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Macromolecule #13: 5'-3' exoribonuclease 2
Macromolecule
Name: 5'-3' exoribonuclease 2 / type: protein_or_peptide / ID: 13 Details: Residues (1M-13M) are also an affinity tag for convenient protein purification. Number of copies: 1 / Enantiomer: LEVO EC number: Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters
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