2024-03-29T01:12:36Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/557752021-11-22T12:55:57Zcom_10261_86com_10261_1col_10261_339
00925njm 22002777a 4500
dc
Klinge, Sebastian
author
Ñez-Ramírez, Rafael
author
Llorca, Óscar
author
Pellegrini, Luca
author
2009-07-08
Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol α, Pol δ and Pol ε. The conserved catalytic and regulatory B subunits associate in a constitutive heterodimer that represents the functional core of all three replicative polymerases. Here, we combine X-ray crystallography and electron microscopy (EM) to describe subunit interaction and 3D architecture of heterodimeric yeast Pol α. The crystal structure of the C-terminal domain (CTD) of the catalytic subunit bound to the B subunit illustrates a conserved mechanism of accessory factor recruitment by replicative polymerases. The EM reconstructions of Pol α reveal a bilobal shape with separate catalytic and regulatory modules. Docking of the B–CTD complex in the EM reconstruction shows that the B subunit is tethered to the polymerase domain through a structured but flexible linker. Our combined findings provide a structural template for the common functional architecture of the three major replicative DNA polymerases
EMBO Journal 28(13):1978-1987(2009)
0261-4189
http://hdl.handle.net/10261/55775
10.1038/emboj.2009.150
1460-2075
19494830
DNA polymerase α
DNA replication
electron microscopy
X-ray crystallography
3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases