Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia

We demonstrate that the Fanconi anemia group G protein is found in mitochondria

Sudit S. Mukhopadhyay; Kathryn S. Leung; M. John Hicks; Philip J. Hastings; Hagop Youssoufian; Sharon E. Plon


Scholarcy highlights

  • The clinical hallmark of Fanconi anemia is the development of pancytopenia in childhood
  • We demonstrate that the FANCG protein interacts physically with PRDX3 and that the proteins colocalize in the mitochondria
  • We present data based on two-hybrid interaction, coimmunoprecipitation, and immunolocalization that the FANCG protein binds and colocalizes with PRDX3 in mitochondria
  • The interaction of these two proteins is lost in the patient-associated G546R-FANCG mutant protein
  • We demonstrated that a portion of FANCG localizes with mitochondria in HeLa and FA-G–corrected cells
  • All FA cells were grown in RPMI and 15% FBS except that the PD352-F fibroblasts were grown in α-MEM and 15% FBS
  • These results suggest that the FANCG protein can translocate into mitochondria and interact with PRDX3
  • 10 μl of labeled PRDX3 protein was incubated with increasing amounts of rat recombinant calpain II or mitochondrial lysates and the activation buffer for 10–15 min at 37°C

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