DNA helicase and helicase–nuclease enzymes with a conserved iron–sulfur cluster

Nucl. Acids Res. (2012) doi: 10.1093/nar/gks039 First published online: January 28, 2012 (This article is Open Access)

Yuliang Wu 1 and Robert M. Brosh Jr 2.
1 Department of Biochemistry, University of Saskatchewan, Health Sciences Building, Saskatoon, Saskatchewan, S7N 5E5, Canada
2 Laboratory of Molecular Gerontology, National Institute on Aging, NIH, NIH Biomedical Research Center, Baltimore, MD 21224, USA

A defect in the synthesis of Fe–S clusters is responsible for mitochondrial dysfunction, leading to nuclear genomic instability (109). Defects in Fe–S assembly due to a deficiency in the iron storage/transport protein frataxin also lead to genomic instability and defective BER (110), suggesting that the conserved Fe–S cluster in Dna2 and other DNA repair/replication proteins may be crippled due to the frataxin deficiency; however, this remains to be shown. Further studies are required to ascertain the importance of the Fe–S staple domain in Dna2 for its nuclear and mitochondrial functions, and the influence of iron homeostasis in this respect.

Full text pdf