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-Structure paper
Title | The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2. |
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Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | Mar 26, 2019 |
Authors | Lucas Tafur / Yashar Sadian / Jonas Hanske / Rene Wetzel / Felix Weis / Christoph W Müller / |
PubMed Abstract | RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first ...RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserved position at the A135 surface. Our structural and biochemical data suggest a mechanism where reversible binding of the A49-A34.5 heterodimer could contribute to the regulation of Pol I transcription initiation and elongation. |
External links | Elife / PubMed:30913026 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.18 - 4.0 Å |
Structure data | EMDB-0238, PDB-6hko: EMDB-0239, PDB-6hlq: EMDB-0240, PDB-6hlr: EMDB-0242: |
Chemicals | ChemComp-MG: ChemComp-ZN: ChemComp-G2P: |
Source |
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Keywords | TRANSCRIPTION / polymerase / nucleotide / elongation / hydrolase |