ZNF524 directly interacts with telomeric DNA and supports telomere integrity

Hanna Braun, Ziyan Xu, Fiona Chang, Nikenza Viceconte, Grishma Rane, Michal Levin, Liudmyla Lototska, Franziska Roth, Alexia Hillairet, Albert Fradera-Sola, Vartika Khanchandani, Zi Wayne Sin, Wai Khang Yong, Oliver Dreesen, Yang Yang, Yunyu Shi, Fudong Li (), Falk Butter () and Dennis Kappei ()
Additional contact information
Hanna Braun: National University of Singapore
Ziyan Xu: University of Science and Technology of China
Fiona Chang: National University of Singapore
Nikenza Viceconte: Institute of Molecular Biology (IMB)
Grishma Rane: National University of Singapore
Michal Levin: Institute of Molecular Biology (IMB)
Liudmyla Lototska: Institute of Molecular Biology (IMB)
Franziska Roth: Institute of Molecular Biology (IMB)
Alexia Hillairet: National University of Singapore
Albert Fradera-Sola: Institute of Molecular Biology (IMB)
Vartika Khanchandani: National University of Singapore
Zi Wayne Sin: National University of Singapore
Wai Khang Yong: National University of Singapore
Oliver Dreesen: Cell Aging Laboratory, A*STAR Skin Research Labs
Yang Yang: University of Science and Technology of China
Yunyu Shi: University of Science and Technology of China
Fudong Li: University of Science and Technology of China
Falk Butter: Institute of Molecular Biology (IMB)
Dennis Kappei: National University of Singapore

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract Telomeres are nucleoprotein structures at the ends of linear chromosomes. In humans, they consist of TTAGGG repeats, which are bound by dedicated proteins such as the shelterin complex. This complex blocks unwanted DNA damage repair at telomeres, e.g. by suppressing nonhomologous end joining (NHEJ) through its subunit TRF2. Here, we describe ZNF524, a zinc finger protein that directly binds telomeric repeats with nanomolar affinity, and reveal base-specific sequence recognition by cocrystallization with telomeric DNA. ZNF524 localizes to telomeres and specifically maintains the presence of the TRF2/RAP1 subcomplex at telomeres without affecting other shelterin members. Loss of ZNF524 concomitantly results in an increase in DNA damage signaling and recombination events. Overall, ZNF524 is a direct telomere-binding protein involved in the maintenance of telomere integrity.

Date: 2023
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DOI: 10.1038/s41467-023-43397-7

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