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-Structure paper
タイトル | Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes. |
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ジャーナル・号・ページ | Cell, Vol. 179, Issue 7, Page 1537-1550.e19, Year 2019 |
掲載日 | 2019年12月12日 |
著者 | Clemens Grimm / Hauke S Hillen / Kristina Bedenk / Julia Bartuli / Simon Neyer / Qian Zhang / Alexander Hüttenhofer / Matthias Erlacher / Christian Dienemann / Andreas Schlosser / Henning Urlaub / Bettina Böttcher / Aladar A Szalay / Patrick Cramer / Utz Fischer / |
PubMed 要旨 | 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 ...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. 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. |
リンク | Cell / PubMed:31835032 |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.897 - 2.76 Å |
構造データ | EMDB-4868, PDB-6rfl: PDB-6rfg: |
化合物 | ChemComp-HOH: ChemComp-ZN: ChemComp-MG: |
由来 |
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キーワード | VIRAL PROTEIN / E11 / E11L / Vaccinia / core protein / RNA Polymerase complex / RNA polymerase / RNAP / vRNAP / complete vRNAP |