We determined the structure of the Polα–primase complex trapped in a DNA elongation state. Cryo-electron microscopy showed that primase has a role in facilitating the timely termination of primer DNA elongation by Polα by hanging on the primer–template complex.
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References
Arezi, B. & Kuchta, R. D. Eukaryotic DNA primase. Trends Biochem. Sci. 25, 572–576 (2000). A review article summarizing transactions within the eukaryotic Polα–primase complex.
Baranovskiy, A. G. et al. Mechanism of concerted RNA–DNA primer synthesis by the human primosome. J. Biol. Chem. 291, 10006–10020 (2016). This paper reports crystal structures of human primosome in apo-form and p58C in complex with a primer–template, and reports biochemical studies of RNA primer length control and its switch from primase to Polα.
He, Q. et al. Structures of the human CST–Polα–primase complex bound to telomere templates. Nature 608, 826–832 (2022). This paper reports the cryo-EM structure of CST–Polα–primase bound to a telomere template in its preinitiation state, and reveals how CST organizes the DNA template and Polα–primase to stimulate RNA primer synthesis.
Baranovskiy, A. G. et al. Insight into the human DNA primase interaction with template-primer. J. Biol. Chem. 291, 4793–4802 (2016). This paper reports how the primer–template interacts with different primase domains and which parts of the primer–template are essential for those interactions.
Baranovskiy, A. G. et al. Insight into RNA–DNA primer length counting by human primosome. Nucleic Acids Res 50, 6264–6270 (2022). This paper reports the role of primosome linkers in the termination of primer synthesis and describes a method for preparing a chimeric RNA–DNA primer with a 5′-triphosphate.
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This is a summary of: He, Q. et al. Structures of human primosome elongation complexes. Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-023-00971-3 (2023).
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Human primase hangs on the primer–template and Polα to facilitate primer termination. Nat Struct Mol Biol 30, 575–576 (2023). https://doi.org/10.1038/s41594-023-00972-2
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DOI: https://doi.org/10.1038/s41594-023-00972-2
