Summary for 8B9C
| Entry DOI | 10.2210/pdb8b9c/pdb |
| EMDB information | 15924 |
| Descriptor | DNA replication licensing factor MCM2, DNA replication complex GINS protein PSF2, DNA replication complex GINS protein PSF3, ... (23 entities in total) |
| Functional Keywords | replication, helicase, polymerase, pol alpha, priming, replisome |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 20 |
| Total formula weight | 1518163.43 |
| Authors | Jones, M.L.,Yeeles, J.T.P. (deposition date: 2022-10-05, release date: 2023-08-09, Last modification date: 2023-08-30) |
| Primary citation | Jones, M.L.,Aria, V.,Baris, Y.,Yeeles, J.T.P. How Pol alpha-primase is targeted to replisomes to prime eukaryotic DNA replication. Mol.Cell, 83:2911-, 2023 Cited by PubMed Abstract: During eukaryotic DNA replication, Pol α-primase generates primers at replication origins to start leading-strand synthesis and every few hundred nucleotides during discontinuous lagging-strand replication. How Pol α-primase is targeted to replication forks to prime DNA synthesis is not fully understood. Here, by determining cryoelectron microscopy (cryo-EM) structures of budding yeast and human replisomes containing Pol α-primase, we reveal a conserved mechanism for the coordination of priming by the replisome. Pol α-primase binds directly to the leading edge of the CMG (CDC45-MCM-GINS) replicative helicase via a complex interaction network. The non-catalytic PRIM2/Pri2 subunit forms two interfaces with CMG that are critical for in vitro DNA replication and yeast cell growth. These interactions position the primase catalytic subunit PRIM1/Pri1 directly above the exit channel for lagging-strand template single-stranded DNA (ssDNA), revealing why priming occurs efficiently only on the lagging-strand template and elucidating a mechanism for Pol α-primase to overcome competition from RPA to initiate primer synthesis. PubMed: 37506699DOI: 10.1016/j.molcel.2023.06.035 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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