Nature research paper: Structures of the human CST-Polα–primase complex bound to telomere templates
RNA-DNA primer for several DNA replication pathwayssuch as lagging-strand synthesis and telomere C-strand fill-in. The underlying physical mechanism of how pol-α/primase, alone or in partnership with accessory proteins, performs its complicated multistep primer synthesis function is unknown. Here, we show that CST, a single-stranded DNA-binding accessory protein complex of pol-α/primase, physically sets up the enzyme for efficient primer synthesis.
Cryo-electron microscopy structures of CST-pol-α/primase preinitiation complex bound to various types of telomere overhang reveal template-bound CST partitions the DNA and RNA catalytic centers of pol-α/primase into two separate domains and effectively arrange them in RNA-DNA synthesis order. The PIC architecture provides a single solution for the multiple structural needs for pol-α/primase RNA-DNA primer synthesis.
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