Nature Genetics
37, 934 - 935 (2005)
Published online: 21 August 2005; | doi:10.1038/ng1625
The DNA helicase BRIP1 is defective in Fanconi anemia complementation group JMarieke Levitus1, 7, Quinten Waisfisz1, 6, 7, Barbara C Godthelp2, 7, Yne de Vries1, Shobbir Hussain3, Wouter W Wiegant2, Elhaam Elghalbzouri-Maghrani2, Jûrgen Steltenpool1, Martin A Rooimans1, Gerard Pals1, Fré Arwert1, Christopher G Mathew3, Ma gorzata Z Zdzienicka2, 4, Kevin Hiom5, Johan P De Winter1
& Hans Joenje11
Department of Clinical Genetics and Human Genetics, VU University Medical Center, Van der Boechorststraat 7, NL-1081 BT
Amsterdam, The Netherlands. 2
Department of Toxicogenetics, Leiden University Medical Center, Wassenaarseweg 72, NL-2333 AL
Leiden, The Netherlands. 3
Division of Genetics and Molecular Medicine, King's College London, Guy's Hospital, London, UK. 4
Department of Molecular Cell Genetics, Nicolaus Copernicus University, Collegium Medicum of L. Rydygier, Bydgoszcz, Poland. 5
MRC Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK. 6
Present address: Department of Hematology, VU University Medical Center, Amsterdam, The Netherlands. 7
These authors contributed equally to this work.
Correspondence should be addressed to Hans Joenje joenje@vumc.nl The protein predicted to be defective in individuals with Fanconi anemia complementation group J (FA-J), FANCJ, is a missing component in the Fanconi anemia pathway of genome maintenance. Here we identify pathogenic mutations in eight individuals with FA-J in the gene encoding the DEAH-box DNA helicase BRIP1, also called FANCJ. This finding is compelling evidence that the Fanconi anemia pathway functions through a direct physical interaction with DNA.
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