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Article
Direct DNA Binding Activity of the Fanconi Anemia D2 Protein
Journal of Biological Chemistry
  • Woo-Hyun Park
  • Steven Margossian
  • Andrew A Horwitz
  • Amanda M Simons, Framingham State University
  • Alan D D'Andrea
  • Jeffrey D Parvin
Document Type
Article
Publication Date
4-23-2005
DOI
10.1074/jbc.M503730200
Version
Citation
Format
Other
Keywords
  • Fanconi anemia D2 protein,
  • FANCD2,
  • Fanconi anemia,
  • DNA,
  • genetics
Subject Categories
Biology
Disciplines
Abstract
It is known that the Fanconi anemia D2 protein is vital for protecting the genome from DNA damage, but what activities this protein has are unknown. In these experiments we purified full-length Fanconi anemia protein D2 (FANCD2), and we found that FANCD2 bound to DNA with specificity for certain structures: double strand DNA ends and Holliday junctions. Proteins containing patient-derived mutations or artificial variants of the FANCD2 protein were similarly expressed and purified, and each variant bound to the Holliday junction DNA with similar affinity as did the wild-type protein. There was no single discrete domain of FANCD2 protein that bound to DNA, but rather the full-length protein was required for structure-specific DNA binding. This finding of DNA binding is the first biochemical activity identified for this key protein in the Fanconi anemia pathway.
Citation Information
Woo-Hyun Park, Steven Margossian, Andrew A Horwitz, Amanda M Simons, et al.. "Direct DNA Binding Activity of the Fanconi Anemia D2 Protein" Journal of Biological Chemistry Vol. 280 (2005) p. 23593 - 23598
Available at: http://works.bepress.com/amanda_simons/4/