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Crystal structure of the human MUS81-EME2 complex

Zhengkang Hua1, Qianqian Fang1, Danping Zhang1

  • 1College of Chemistry, Fuzhou University, Fuzhou 350108, China.

Structure (London, England : 1993)
|March 15, 2022
PubMed

Insights

The crystal structure of the MUS81-EME2 complex was determined, revealing similarities to MUS81-EME1. Biochemical studies show both complexes have identical DNA processing activities, suggesting cellular timing dictates their distinct roles.

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • MUS81 is a crucial structure-specific endonuclease involved in DNA repair.
  • In humans, MUS81 forms complexes with EME1 and EME2, with distinct roles in cell cycle phases.
  • The structure of MUS81-EME1 is known, but MUS81-EME2 remains uncharacterized.

Purpose of the Study:

  • To determine the crystal structure of the human MUS81-EME2 complex.
  • To compare the biochemical activities and substrate recognition of MUS81-EME1 and MUS81-EME2 complexes.
  • To elucidate the structural basis for DNA substrate recognition by MUS81-EME endonucleases.

Main Methods:

  • X-ray crystallography to determine the MUS81-EME2 structure.
  • Biochemical assays to assess endonuclease activity and substrate specificity.
  • Structure-guided mutagenesis to investigate DNA binding interactions.

Main Results:

  • The crystal structure of MUS81-EME2 was solved, showing a fold similar to MUS81-EME1.
  • In vitro biochemical assays demonstrated identical substrate recognition and endonuclease activities for both MUS81-EME1 and MUS81-EME2 complexes.
  • Structure-guided mutagenesis provided insights into the molecular mechanisms of DNA substrate binding.

Conclusions:

  • The structural similarity and identical in vitro activities suggest that the distinct cellular functions of MUS81-EME1 and MUS81-EME2 complexes are likely regulated by temporal controls within the cell.
  • This study provides a structural foundation for understanding how MUS81-EME endonucleases recognize diverse DNA structures.
Keywords:
DNA damage repairEME2Holliday junctionMUS81crystal structurehomologous recombinationstructure-specific endonucleasesubstrate specificity

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