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Updated: Feb 11, 2026

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The BUB3-BUB1 Complex Promotes Telomere DNA Replication.

Feng Li1, Hyeung Kim2, Zhejian Ji3

  • 1Key Laboratory of Gene Engineering of the Ministry of Education and State Key Laboratory of Oncology in South China, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, China.

Molecular Cell
|May 5, 2018
PubMed
Summary
This summary is machine-generated.

The BUB3-BUB1 complex binds telomeres during S phase, promoting DNA replication and preventing fragile, shortened telomeres. This discovery reveals new roles for the spindle assembly checkpoint in maintaining genome integrity.

Keywords:
BLMBUB 3BUB1DNA replicationTRF1TRF2telomeretelomere length

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Area of Science:

  • Cell Biology
  • Genetics
  • Molecular Biology

Background:

  • Telomeres form nucleoprotein structures essential for genome integrity.
  • Telomere replication during S phase presents challenges that are not fully understood.
  • Replication stress at telomeres can lead to genomic instability.

Purpose of the Study:

  • To investigate the role of the BUB3-BUB1 complex in telomere DNA replication during S phase.
  • To elucidate the mechanism by which BUB3-BUB1 functions at telomeres.
  • To identify factors that regulate BUB3-BUB1 localization and activity at telomeres.

Main Methods:

  • Telomere binding assays to detect BUB3-BUB1 at telomeres during S phase.
  • Analysis of telomere length and integrity in cells lacking the BUB3-BUB1 complex.
  • Biochemical assays to assess the telomere-binding and kinase activities of BUB3 and BUB1.
  • Investigating the interaction between TRF2, BUB1-BUB3, TRF1, and BLM helicase.

Main Results:

  • The BUB3-BUB1 complex localizes to telomeres during S phase and promotes DNA replication.
  • Loss of BUB3-BUB1 leads to telomere replication defects, including fragility and shortening.
  • Telomere binding of BUB3 and kinase activity of BUB1 are crucial for their telomeric function.
  • TRF2 facilitates BUB1-BUB3 recruitment to telomeres, where BUB1 phosphorylates TRF1 and recruits BLM helicase to resolve replication stress.

Conclusions:

  • The BUB3-BUB1 complex plays a novel and critical role in S phase telomere replication.
  • Coordination between spindle assembly checkpoint proteins and telomere-specific factors ensures telomere maintenance.
  • These findings provide new insights into the resolution of telomere replication stress and genome stability.