Rapid dynamics allow the low-abundance RTEL1 helicase to promote telomere replication.

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Tác giả: Nausica Arnoult, Thomas R Cech, Erin Taylor, Guanhui Wu, Daniel T Youmans

Ngôn ngữ: eng

Ký hiệu phân loại: 025.29 Acquisition of and collection development for materials from geographic areas

Thông tin xuất bản: England : Nucleic acids research , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 712802

Regulator of telomere length 1 (RTEL1) helicase facilitates telomere replication by disassembling DNA secondary structures, such as G-quadruplexes and telomeric loops (t-loops), at the ends of the chromosomes. The recruitment of RTEL1 to telomeres occurs during the S-phase of the cell cycle, but the dynamics of the process has not been studied. Here, we utilized CRISPR genome editing and single-molecule imaging to monitor RTEL1 movement within human cell nuclei. RTEL1 utilizes rapid three-dimensional diffusion to search for telomeres and other nuclear targets. Only 5% of the chromatin-bound RTEL1 is associated with telomeres at any time in the S-phase, but the telomere-bound RTEL1 has much more extended associations. This binding is enhanced by the interaction between RTEL1 and the telomeric protein TRF2 but is largely independent of RTEL1 ATPase activity. The absence of RTEL1 catalytic activity leads to severe defects in cell proliferation, slow progression out of S-phase, and chromosome end-to-end fusion events. We propose that the rapid diffusion of RTEL1 allows this low-abundance protein to explore the nucleus, bind TRF2, and be recruited to telomeres.
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