bioRxivBiochemistry
Cryo-EM structure of the human CST·Polα/Primase complex in a recruitment state
S. W. Cai, J. C. Zinder, V. Svetlov, M. Bush, E. Nudler, T. Walz, T. de Lange
Abstract
The CST*Pol/Primase complex is essential for telomere overhang maintenance and additionally functions to counteract resection at double-strand breaks. We report a 4.6-[A] resolution cryo-EM structure of CST*Pol/Primase, captured prior to catalysis in a recruitment state, which provides insights into the architecture and stoichiometry of the fill-in machinery. Our model informs on human disease mutations that cause Coats plus syndrome.
- organism: human
- assay: cryo-EM
- research focus: protein structure prediction
- approach: experimental assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- POT1 recruits and regulates CST-Polα/Primase at human telomeres
S. W. Cai, H. Takai, … T. de Lange·bioRxiv·May 8, 2023
- Structure of human CST-pol-α/primase bound to a telomeric overhang poised for initiation of telomere C-strand synthesis
- Structure of telomerase-bound CST with Polymerase α-Primase
Yao He, He Song, … Juli F. Feigon·bioRxiv·Dec 28, 2021
- The yeast CST and Polα/primase complexes act in concert to ensure proper telomere maintenance and protection
Kimberly Calugaru, Eun Young Yu, … Neal F. Lue·Nucleic Acids ResearchPeer-reviewed·Mar 19, 2025
- CST does not evict elongating telomerase but prevents initiation by ssDNA binding
A. J. Zaug, C. J. Lim, … T. R. Cech·Nucleic Acids ResearchPeer-reviewed·Oct 28, 2021
- The cryo-EM structure of human CST reveals a two-megadalton decameric assembly bound to telomeric DNA
C. J. Lim, A. T. Barbour, … T. R. Cech·bioRxiv·Oct 23, 2019