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-Structure paper
Title | 3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases. |
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Journal, issue, pages | EMBO J, Vol. 28, Issue 13, Page 1978-1987, Year 2009 |
Publish date | Jul 8, 2009 |
Authors | Sebastian Klinge / Rafael Núñez-Ramírez / Oscar Llorca / Luca Pellegrini / |
PubMed Abstract | Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol alpha, Pol delta and Pol epsilon. The conserved catalytic and regulatory B subunits associate in ...Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol alpha, Pol delta and Pol epsilon. 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 alpha. 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 alpha 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. |
External links | EMBO J / PubMed:19494830 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.5 - 22.9 Å |
Structure data | EMDB-1618: PDB-3flo: |
Chemicals | ChemComp-SO4: ChemComp-ZN: ChemComp-HOH: |
Source |
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Keywords | TRANSFERASE / Protein-protein complex / phosphoesterase fold / OB fold / Zinc-binding motif / DNA replication / Nucleus / Phosphoprotein / DNA-binding / DNA-directed DNA polymerase / Nucleotidyltransferase |