4B08

Yeast DNA polymerase alpha, Selenomethionine protein

Summary for 4B08

• Entry DOI: 10.2210/pdb4b08/pdb
• Related: 4FVM 4FXD 4FYD
• Descriptor: DNA POLYMERASE ALPHA CATALYTIC SUBUNIT A (2 entities in total)
• Functional Keywords: transferase, dna polymerase, dna replication
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P13382
• Total number of polymer chains: 1
• Total formula weight: 104844.91

Authors

Perera, R.L.,Torella, R.,Klinge, S.,Kilkenny, M.L.,Maman, J.D.,Pellegrini, L. (deposition date: 2012-06-29, release date: 2013-02-27, Last modification date: 2024-10-09)

Primary citation

Perera, R.L.,Torella, R.,Klinge, S.,Kilkenny, M.L.,Maman, J.D.,Pellegrini, L.
Mechanism for Priming DNA Synthesis by Yeast DNA Polymerase Alpha
Elife, 2:482-, 2013

PubMed Abstract: The DNA Polymerase α (Pol α)/primase complex initiates DNA synthesis in eukaryotic replication. In the complex, Pol α and primase cooperate in the production of RNA-DNA oligonucleotides that prime synthesis of new DNA. Here we report crystal structures of the catalytic core of yeast Pol α in unliganded form, bound to an RNA primer/DNA template and extending an RNA primer with deoxynucleotides. We combine the structural analysis with biochemical and computational data to demonstrate that Pol α specifically recognizes the A-form RNA/DNA helix and that the ensuing synthesis of B-form DNA terminates primer synthesis. The spontaneous release of the completed RNA-DNA primer by the Pol α/primase complex simplifies current models of primer transfer to leading- and lagging strand polymerases. The proposed mechanism of nucleotide polymerization by Pol α might contribute to genomic stability by limiting the amount of inaccurate DNA to be corrected at the start of each Okazaki fragment. DOI:http://dx.doi.org/10.7554/eLife.00482.001.

PubMed: 23599895
DOI: 10.7554/ELIFE.00482

Experimental method

X-RAY DIFFRACTION (2.67 Å)