Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes | Zendy

Clemens Grimm | Zendy; Hauke S. Hillen | Zendy; Kristina Bedenk | Zendy; J. Bartuli | Zendy; Simon Neyer | Zendy; Qian Zhang | Zendy; Alexander Hüttenhofer | Zendy; Matthias David Erlacher | Zendy; Christian Dienemann | Zendy; Andreas Schlösser | Zendy; Henning Urlaub | Zendy; Bettina Böttcher | Zendy; Aladar A. Szalay | Zendy; Patrick Cramer | Zendy; Utz Fischer | Zendy

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Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes

Author(s) -

Clemens Grimm,

Hauke S. Hillen,

Kristina Bedenk,

J. Bartuli,

Simon Neyer,

Qian Zhang,

Alexander Hüttenhofer,

Matthias David Erlacher,

Christian Dienemann,

Andreas Schlösser,

Henning Urlaub,

Bettina Böttcher,

Aladar A. Szalay,

Patrick Cramer,

Utz Fischer

Publication year - 2019

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2019.11.024

Subject(s) - biology , rna polymerase ii , transcription factor ii b , transcription factor ii d , transcription factor ii f , rna polymerase ii holoenzyme , polymerase , transcription (linguistics) , rna polymerase , processivity , microbiology and biotechnology , rna polymerase i , general transcription factor , rna polymerase iii , termination factor , rna , rna dependent rna polymerase , virology , genetics , dna , gene expression , gene , promoter , linguistics , philosophy

Poxviruses encode a multisubunit DNA-dependent RNA polymerase (vRNAP) that carries out viral gene expression in the host cytoplasm. We report cryo-EM structures of core and complete vRNAP enzymes from Vaccinia virus at 2.8 Å resolution. The vRNAP core enzyme resembles eukaryotic RNA polymerase II (Pol II) but also reveals many virus-specific features, including the transcription factor Rap94. The complete enzyme additionally contains the transcription factor VETF, the mRNA processing factors VTF/CE and NPH-I, the viral core protein E11, and host tRNA Gln . This complex can carry out the entire early transcription cycle. The structures show that Rap94 partially resembles the Pol II initiation factor TFIIB, that the vRNAP subunit Rpo30 resembles the Pol II elongation factor TFIIS, and that NPH-I resembles chromatin remodeling enzymes. Together with the accompanying paper (Hillen et al., 2019), these results provide the basis for unraveling the mechanisms of poxvirus transcription and RNA processing.

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