The structure of human CST reveals a decameric assembly bound to telomeric DNA.
作者： Ci Ji Lim , Alexandra T. Barbour , Arthur J. Zaug , Karen J. Goodrich , Allison E. McKay
关键词:
摘要: The CTC1-STN1-TEN1 (CST) complex is essential for telomere maintenance and resolution of stalled replication forks genome-wide. Here, we report the 3.0-angstrom cryo-electron microscopy structure human CST bound to telomeric single-stranded DNA (ssDNA), which assembles as a decameric supercomplex. atomic model 134-kilodalton CTC1 subunit, built almost entirely de novo, reveals overall architecture DNA-binding anchor site. carboxyl-terminal domain STN1 interacts with at two separate docking sites, allowing allosteric mediation decamer assembly. Furthermore, ssDNA appears staple monomers nucleate has stronger structural similarity Replication Protein A than expected yeast Cdc13. suggests that can organize analogously nucleosome's organization double-stranded DNA.
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