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

Nucleic Acids Res. 2012 May;40(10):4247-60. doi: 10.1093/nar/gks039. Epub 2012 Jan 28.


Conserved Iron-Sulfur (Fe-S) clusters are found in a growing family of metalloproteins that are implicated in prokaryotic and eukaryotic DNA replication and repair. Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases characterized by DNA repair defects and/or a poor response to replication stress. Insight to the structural and functional importance of the conserved Fe-S domain in DNA helicases has been gleaned from structural studies of the purified proteins and characterization of Fe-S cluster site-directed mutants. In this review, we will provide a current perspective of what is known about the Fe-S cluster helicases, with an emphasis on how the conserved redox active domain may facilitate mechanistic aspects of helicase function. We will discuss testable models for how the conserved Fe-S cluster might operate in helicase and helicase-nuclease enzymes to conduct their specialized functions that help to preserve the integrity of the genome.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • DNA / metabolism
  • DNA Glycosylases / chemistry
  • DNA Helicases / chemistry*
  • DNA Helicases / metabolism
  • DNA Primase / chemistry
  • Deoxyribonucleases / chemistry*
  • Deoxyribonucleases / metabolism
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / metabolism
  • Molecular Sequence Data
  • Protein Structure, Tertiary


  • Iron-Sulfur Proteins
  • DNA
  • DNA Primase
  • Deoxyribonucleases
  • DNA Glycosylases
  • DNA Helicases