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Integrating structural dynamics and functional diversity of archaeal Mre11 proteins in DNA repair: A review

Tian Gao1, Yaqi Zheng1, Botao Zhang2

  • 1College of Environmental Science and Engineering, Yangzhou University, Yangzhou City 210095, China.

International Journal of Biological Macromolecules
|July 10, 2025
PubMed

Insights

Archaeal Mre11 proteins, crucial for DNA double-stranded break repair, show diverse functions and mechanisms shaped by extreme environments. Understanding these differences offers insights into DNA repair and adaptation.

Area of Science:

  • Molecular Biology
  • Genomics
  • Biochemistry

Background:

  • DNA double-stranded breaks (DSBs) are cytotoxic lesions essential for maintaining genomic stability.
  • Mre11 protein, partnered with Rad50, is conserved across life and drives DSB repair via homologous recombination.
  • Mre11 possesses dual enzymatic activities and a tripartite architecture, but archaeal homologs display functional divergence.

Purpose of the Study:

  • To review recent advances on archaeal Mre11 proteins.
  • To focus on functional differences between archaeal species and other organisms.
  • To understand the structure-function relationship of archaeal Mre11 proteins.

Main Methods:

  • Review of existing literature on archaeal Mre11 proteins.
  • Comparative analysis of Mre11 functions and repair mechanisms across archaeal species.
  • Examination of Mre11 structure-function relationships in different organisms.

Main Results:

  • Six archaeal Mre11 proteins exhibit distinct functions and repair mechanisms.
  • Functional divergence in archaeal Mre11 is likely influenced by extreme environmental pressures.
  • Differences highlight a balance between conserved and lineage-specific adaptations in Mre11 evolution.

Conclusions:

  • Archaeal Mre11 proteins present a unique model for studying DNA repair evolution.
  • Investigating these proteins offers novel insights into DNA repair biology and adaptation.
  • Future research should explore the interplay of conservation and adaptation in archaeal Mre11.
Keywords:
ArchaeaHomologous recombinationMre11 protein

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