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Structures of the human CST-Polα–primase complex bound to telomere templates
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Structures of the human CST-Polα–primase complex bound to telomere templates
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Journal Article
Structures of the human CST-Polα–primase complex bound to telomere templates
2022
Overview
The mammalian DNA polymerase-α–primase (Polα–primase) complex is essential for DNA metabolism, providing the de novo RNA–DNA primer for several DNA replication pathways
1
–
4
such as lagging-strand synthesis and telomere C-strand fill-in. The physical mechanism underlying how Polα–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 for Polα–primase, physically organizes the enzyme for efficient primer synthesis. Cryogenic electron microscopy structures of the CST-Polα–primase preinitiation complex (PIC) bound to various types of telomere overhang reveal that template-bound CST partitions the DNA and RNA catalytic centres of Polα–primase into two separate domains and effectively arranges them in RNA–DNA synthesis order. The architecture of the PIC provides a single solution for the multiple structural requirements for the synthesis of RNA–DNA primers by Polα–primase. Several insights into the template-binding specificity of CST, template requirement for assembly of the CST-Polα–primase PIC and activation are also revealed in this study.
A structural analysis demonstrates how the single-stranded DNA-binding accessory protein complex CST physically organizes the human DNA polymerase-α–primase complex for efficient primer synthesis during telomere replication.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ 82/29
/ Binding
/ DNA
/ Enzymes
/ Genomes
/ Humanities and Social Sciences
/ Humans
/ Primase
/ Proteins
/ RNA
/ Science
/ Shelterin Complex - chemistry
