Structural basis of poxvirus transcription: Vaccinia RNA polymerase complexes.

Grimm, C.; Hillen, H. S.; Bedenk, K.; Bartuli, J.; Neyer, S.; Zhang, Q.; Hüttenhofer, A.; Erlacher, M.; Dienemann, C.; Schlosser, A.; Urlaub, H.; Böttcher, B.; Szalay, A. A.; Cramer, P.; Fischer, U.

doi:10.1016/j.cell.2019.11.024

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

このアイテムの新しいバージョンが利用可能です:
https://pure.mpg.de/pubman/item/item_3182509_3

詳細要約

公開

学術論文

Structural basis of poxvirus transcription: Vaccinia RNA polymerase complexes.

MPS-Authors

/persons/resource/persons211404

Hillen, H. S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons200231

Neyer, S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons195449

Dienemann, C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub, H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons127020

Cramer, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Grimm, C., Hillen, H. S., Bedenk, K., Bartuli, J., Neyer, S., Zhang, Q., Hüttenhofer, A., Erlacher, M., Dienemann, C., Schlosser, A., Urlaub, H., Böttcher, B., Szalay, A. A., Cramer, P., & Fischer, U. (2019). Structural basis of poxvirus transcription: Vaccinia RNA polymerase complexes. Cell, 179(7), 1537-1550. doi:10.1016/j.cell.2019.11.024.

引用: https://hdl.handle.net/21.11116/0000-0005-5D8D-5

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 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 tRNAGln. 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.