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Structure-function relationships of the Mre11 protein in the control of DNA end bridging and processing

Antonio Marsella1, Corinne Cassani1, Erika Casari1

  • 1Dipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.

Current Genetics
|June 21, 2018
PubMed

Insights

The Mre11-Rad50-Xrs2 (MRX) complex and Sae2 protein are crucial for DNA double-strand break (DSB) repair. This study reveals distinct Mre11 domains mediate different resistance functions, impacting DSB resection and tethering.

Area of Science:

  • Molecular Biology
  • Genetics
  • DNA Repair Mechanisms

Background:

  • The Mre11-Rad50-Xrs2 (MRX) complex and Sae2 protein are essential for initiating DNA double-strand break (DSB) repair.
  • These proteins cooperate in DNA end resection and tethering, but their precise roles in DNA damage resistance are unclear.

Purpose of the Study:

  • To elucidate the specific functions of the MRX-Sae2 complex in DNA damage resistance.
  • To investigate how different structural domains of Mre11 contribute to cellular resistance against genotoxic agents.

Main Methods:

  • Utilized mre11 alleles that suppress sae2∆ cell hypersensitivity to genotoxic agents.
  • Investigated the roles of Mre11's N-terminal and C-terminal domains in DNA repair processes.

Main Results:

  • Identified two distinct functional domains within Mre11 that mediate resistance to genotoxic agents.
  • The Mre11 N-terminal domain facilitates MRX and Tel1/ATM association with DSBs, impacting resection.
  • The Mre11 C-terminus mediates MRX-tethering activity through Rad50 interaction.

Conclusions:

  • Mre11's distinct domains play separable roles in DNA double-strand break repair and resistance.
  • Understanding these domain functions provides insights into MRX complex roles in DNA repair and potential implications for human diseases.
Keywords:
DNA damageMre11Rad50ResectionSae2Tel1

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