The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding
The catalytic subunit E9 of the vaccinia virus DNA polymerase forms a functional polymerase holoenzyme by interacting with the heterodimeric processivity factor A20/D4. Here the authors present the structure of full-length E9 and show that an insertion within its palm domain binds A20, in a mode dif...
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Nature Portfolio
2017
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oai:doaj.org-article:c56c0fb397134f73a47946a17d780b072021-12-02T15:38:58ZThe vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding10.1038/s41467-017-01542-z2041-1723https://doaj.org/article/c56c0fb397134f73a47946a17d780b072017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01542-zhttps://doaj.org/toc/2041-1723The catalytic subunit E9 of the vaccinia virus DNA polymerase forms a functional polymerase holoenzyme by interacting with the heterodimeric processivity factor A20/D4. Here the authors present the structure of full-length E9 and show that an insertion within its palm domain binds A20, in a mode different from other family B polymerases.Nicolas TarbouriechCorinne DucournauStephanie HutinPhilippe J. MasPetr ManEric ForestDarren J. HartChristophe N. PeyrefitteWim P. BurmeisterFrédéric IseniNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017) |
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DOAJ |
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DOAJ |
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EN |
| topic |
Science Q |
| spellingShingle |
Science Q Nicolas Tarbouriech Corinne Ducournau Stephanie Hutin Philippe J. Mas Petr Man Eric Forest Darren J. Hart Christophe N. Peyrefitte Wim P. Burmeister Frédéric Iseni The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| description |
The catalytic subunit E9 of the vaccinia virus DNA polymerase forms a functional polymerase holoenzyme by interacting with the heterodimeric processivity factor A20/D4. Here the authors present the structure of full-length E9 and show that an insertion within its palm domain binds A20, in a mode different from other family B polymerases. |
| format |
article |
| author |
Nicolas Tarbouriech Corinne Ducournau Stephanie Hutin Philippe J. Mas Petr Man Eric Forest Darren J. Hart Christophe N. Peyrefitte Wim P. Burmeister Frédéric Iseni |
| author_facet |
Nicolas Tarbouriech Corinne Ducournau Stephanie Hutin Philippe J. Mas Petr Man Eric Forest Darren J. Hart Christophe N. Peyrefitte Wim P. Burmeister Frédéric Iseni |
| author_sort |
Nicolas Tarbouriech |
| title |
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| title_short |
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| title_full |
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| title_fullStr |
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| title_full_unstemmed |
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| title_sort |
vaccinia virus dna polymerase structure provides insights into the mode of processivity factor binding |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/c56c0fb397134f73a47946a17d780b07 |
| work_keys_str_mv |
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