Structural highlights
Function
[DPOA2_YEAST] Non-catalytic component of DNA polymerase alpha, which in a complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL12 may play an essential role at the early stage of chromosomal DNA replication by coupling DNA polymerase alpha to the cellular replication machinery (By similarity). Interacts with MCM10. [DPOA_YEAST] Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases.,Klinge S, Nunez-Ramirez R, Llorca O, Pellegrini L EMBO J. 2009 Jul 8;28(13):1978-87. Epub 2009 Jun 4. PMID:19494830[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Qi H, Zakian VA. The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein. Genes Dev. 2000 Jul 15;14(14):1777-88. PMID:10898792
- ↑ Klinge S, Nunez-Ramirez R, Llorca O, Pellegrini L. 3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases. EMBO J. 2009 Jul 8;28(13):1978-87. Epub 2009 Jun 4. PMID:19494830 doi:10.1038/emboj.2009.150
