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Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response

Yucai Wang1, Xiao Han, Fangming Wu

  • 1Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.

Cell Research
|September 4, 2013
PubMed

Insights

The FANCM/FAAP24 complex protects cells from DNA damage. This study reveals FAAP24

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The FANCM/FAAP24 heterodimer is crucial for cellular defense against complex DNA lesions like interstrand crosslinks.
  • Its protective functions depend on recognizing and binding damaged DNA or stalled replication forks, but FAAP24's specific DNA-binding role was unclear.

Purpose of the Study:

  • To elucidate the contribution of FAAP24 to the DNA-interacting functions of the FANCM/FAAP24 complex.
  • To characterize the structural and functional aspects of FAAP24's interaction with DNA.

Main Methods:

  • Acquisition of N-terminal and C-terminal solution structures of human FAAP24.
  • In silico modeling to predict DNA-binding affinity.
  • In vitro and in vivo functional assays using FAAP24 mutants.

Main Results:

  • Structural modeling suggested FAAP24 has high affinity for single-stranded DNA (ssDNA).
  • Mutational analyses confirmed FAAP24's ssDNA-binding capability.
  • Distinct mutations affecting DNA-binding versus FANCM interaction identified, both requiring the C-terminal (HhH)2 domain.

Conclusions:

  • FAAP24 plays dual roles in the DNA damage response to crosslinking lesions.
  • These roles include heterodimer formation with FANCM and direct ssDNA binding for checkpoint activation.

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