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TitleInsights into POT1 structural dynamics revealed by cryo-EM.
Journal, issue, pagesPLoS One, Vol. 17, Issue 2, Page e0264073, Year 2022
Publish dateFeb 17, 2022
AuthorsEmmanuel W Smith / Simon Lattmann / Zhehui Barry Liu / Bilal Ahsan / Daniela Rhodes /
PubMed AbstractTelomeres are protein-DNA complexes that protect the ends of linear eukaryotic chromosomes. Mammalian telomeric DNA consists of 5'-(TTAGGG)n-3' double-stranded repeats, followed by up to several ...Telomeres are protein-DNA complexes that protect the ends of linear eukaryotic chromosomes. Mammalian telomeric DNA consists of 5'-(TTAGGG)n-3' double-stranded repeats, followed by up to several hundred bases of a 3' single-stranded G-rich overhang. The G-rich overhang is bound by the shelterin component POT1 which interacts with TPP1, the component involved in telomerase recruitment. A previously published crystal structure of the POT1 N-terminal half bound to the high affinity telomeric ligand 5'-TTAGGGTTAG-3' showed that the first six nucleotides, TTAGGG, are bound by the OB1 fold, while the adjacent OB2 binds the last four, TTAG. Here, we report two cryo-EM structures of full-length POT1 bound by the POT1-binding domain of TPP1. The structures differ in the relative orientation of the POT1 OB1 and OB2, suggesting that these two DNA-binding OB folds take up alternative conformations. Supporting DNA binding studies using telomeric ligands in which the OB1 and OB2 binding sites were spaced apart, show that POT1 binds with similar affinities to spaced or contiguous binding sites, suggesting plasticity in DNA binding and a role for the alternative conformations observed. A likely explanation is that the structural flexibility of POT1 enhances binding to the tandemly arranged telomeric repeats and hence increases telomere protection.
External linksPLoS One / PubMed:35176105 / PubMed Central
MethodsEM (single particle)
Resolution7.9 - 9.6 Å
Structure data

EMDB-30596:
Cryo-EM map of POT1 bound by TPP1 in closed conformation
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-30597:
Cryo-EM map of POT1 bound by TPP1 in extended conformation
Method: EM (single particle) / Resolution: 9.6 Å

Source
  • Homo sapiens (human)

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