| Registro completo |
| Provedor de dados: |
ArchiMer
|
| País: |
France
|
| Título: |
Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography
|
| Autores: |
Sauguet, Ludovic
Raia, Pierre
Henneke, Ghislaine
Delarue, Marc
|
| Data: |
2016-08
|
| Ano: |
2016
|
| Resumo: |
Archaeal replicative DNA polymerase D (PolD) constitute an atypical class of DNA polymerases made of a proofreading exonuclease subunit (DP1) and a larger polymerase catalytic subunit (DP2), both with unknown structures. We have determined the crystal structures of Pyrococcus abyssi DP1 and DP2 at 2.5 and 2.2 angstrom resolution, respectively, revealing a catalytic core strikingly different from all other known DNA polymerases (DNAPs). Rather, the PolD DP2 catalytic core has the same 'double-psi beta-barrel' architecture seen in the RNA polymerase (RNAP) superfamily, which includes multi-subunit transcriptases of all domains of life, homodimeric RNA-silencing pathway RNAPs and atypical viral RNAPs. This finding bridges together, in non-viral world, DNA transcription and DNA replication within the same protein superfamily. This study documents further the complex evolutionary history of the DNA replication apparatus in different domains of life and proposes a classification of all extant DNAPs.
|
| Tipo: |
Text
|
| Idioma: |
Inglês
|
| Identificador: |
http://archimer.ifremer.fr/doc/00350/46144/45842.pdf
DOI:10.1038/ncomms12227
http://archimer.ifremer.fr/doc/00350/46144/
|
| Editor: |
Nature Publishing Group
|
| Formato: |
application/pdf
|
| Fonte: |
Nature Communications (2041-1723) (Nature Publishing Group), 2016-08 , Vol. 7 , N. 12227 , P. 1-12
|
| Direitos: |
The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material.
info:eu-repo/semantics/openAccess
restricted use
|
|
