Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes

被引:39
作者
Grimm, Clemens [1 ,2 ]
Hillen, Hauke S. [3 ]
Bedenk, Kristina [1 ,2 ]
Bartuli, Julia [1 ,2 ]
Neyer, Simon [3 ]
Zhang, Qian [6 ]
Huettenhofer, Alexander [7 ]
Erlacher, Matthias [7 ]
Dienemann, Christian [3 ]
Schlosser, Andreas [8 ]
Urlaub, Henning [4 ,5 ]
Boettcher, Bettina [1 ,2 ,8 ]
Szalay, Aladar A. [1 ,2 ,6 ]
Cramer, Patrick [3 ]
Fischer, Utz [1 ,2 ,6 ,9 ,10 ]
机构
[1] Univ Wurzburg, Dept Biochem, D-97074 Wurzburg, Germany
[2] Univ Wurzburg, Canc Therapy Res Ctr, Theodor Boveri Inst, D-97074 Wurzburg, Germany
[3] Max Planck Inst Biophys Chem, Dept Mol Biol, Fassberg 11, D-37077 Gottingen, Germany
[4] Max Planck Inst Biophys Chem, Bioanalyt Mass Spectrometry Grp, Fassberg 11, D-37077 Gottingen, Germany
[5] Univ Med Ctr Gottingen, Inst Clin Chem, Bioanalyt, Robert Koch Str 40, D-37075 Gottingen, Germany
[6] Genelux Corp, 3030 Bunker Hill St, San Diego, CA 92109 USA
[7] Med Univ Innsbruck, Bioctr, Div Genom & RNom, A-6020 Innsbruck, Austria
[8] Univ Wurzburg, Rudolf Virchow Ctr, Josef Schneider Str 4, D-97080 Wurzburg, Germany
[9] Helmholtz Inst RNA Based Infect Res HIRI, D-97080 Wurzburg, Germany
[10] Helmholtz Ctr Infect Res HZI, D-97080 Wurzburg, Germany
基金
欧洲研究理事会; 英国生物技术与生命科学研究理事会; 奥地利科学基金会;
关键词
TRIPHOSPHATE PHOSPHOHYDROLASE-I; VIRUS EARLY TRANSCRIPTION; TEMPERATURE-SENSITIVE MUTATIONS; CARBOXY-TERMINAL DOMAIN; CRYSTAL-STRUCTURE; MESSENGER-RNA; CAPPING ENZYME; H4L SUBUNIT; ELONGATION COMPLEX; CLEAVAGE FACTOR;
D O I
10.1016/j.cell.2019.11.024
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Poxviruses encode a multisubunit DNA-dependent RNA polymerase (vRNAP) that carries out viral gene expression in the host cytoplasm. We report cryoEM structures of core and complete vRNAP enzymes from Vaccinia virus at 2.8 angstrom 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.
引用
收藏
页码:1537 / +
页数:33
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