Abstract:
:POT1 and TPP1 are part of the shelterin complex and are essential for telomere length regulation and maintenance. Naturally occurring mutations of the telomeric POT1-TPP1 complex are implicated in familial glioma, melanoma and chronic lymphocytic leukaemia. Here we report the atomic structure of the interacting portion of the human telomeric POT1-TPP1 complex and suggest how several of these mutations contribute to malignant cancer. The POT1 C-terminus (POT1C) forms a bilobal structure consisting of an OB-fold and a holiday junction resolvase domain. TPP1 consists of several loops and helices involved in extensive interactions with POT1C. Biochemical data shows that several of the cancer-associated mutations, partially disrupt the POT1-TPP1 complex, which affects its ability to bind telomeric DNA efficiently. A defective POT1-TPP1 complex leads to longer and fragile telomeres, which in turn promotes genomic instability and cancer.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Rice C,Shastrula PK,Kossenkov AV,Hills R,Baird DM,Showe LC,Doukov T,Janicki S,Skordalakes Edoi
10.1038/ncomms14928subject
Has Abstractpub_date
2017-04-10 00:00:00pages
14928issn
2041-1723pii
ncomms14928journal_volume
8pub_type
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