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TitlePOT1 recruits and regulates CST-Polα/Primase at human telomeres.
Journal, issue, pagesbioRxiv, Year 2023
Publish dateOct 26, 2023
AuthorsSarah W Cai / Hiroyuki Takai / Thomas Walz / Titia de Lange /
PubMed AbstractTelomere maintenance requires extension of the G-rich telomeric repeat strand by telomerase and fill-in synthesis of the C-rich strand by Polα/Primase. Telomeric Polα/Primase is bound to Ctc1-Stn1- ...Telomere maintenance requires extension of the G-rich telomeric repeat strand by telomerase and fill-in synthesis of the C-rich strand by Polα/Primase. Telomeric Polα/Primase is bound to Ctc1-Stn1-Ten1 (CST), a single-stranded DNA-binding complex. Like mutations in telomerase, mutations affecting CST-Polα/Primase result in pathological telomere shortening and cause a telomere biology disorder, Coats plus (CP). We determined cryogenic electron microscopy structures of human CST bound to the shelterin heterodimer POT1/TPP1 that reveal how CST is recruited to telomeres by POT1. Phosphorylation of POT1 is required for CST recruitment, and the complex is formed through conserved interactions involving several residues mutated in CP. Our structural and biochemical data suggest that phosphorylated POT1 holds CST-Polα/Primase in an inactive auto-inhibited state until telomerase has extended the telomere ends. We propose that dephosphorylation of POT1 releases CST-Polα/Primase into an active state that completes telomere replication through fill-in synthesis.
External linksbioRxiv / PubMed:37215005 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.1 Å
Structure data

40659

8soj

EMDB-40659, PDB-8soj:
Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
Method: EM (single particle) / Resolution: 3.8 Å

40660

8sok

EMDB-40660, PDB-8sok:
Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • escherichia coli o157:h7 (bacteria)
  • human enterovirus 71
KeywordsDNA BINDING PROTEIN / telomere / shelterin / cst / complex

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