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Papers In Press, published online ahead of print December 18, 2001
University of Pittsburgh Cancer Institute, University of Pittsburgh, Pittsburgh, PA 15261
Corresponding Author: rdwood{at}pitt.edu
Repair of DNA interstrand crosslinks is a challenging problem for cells. Many human gene products influence sensitivity to DNA crosslinking agents, but the mechanisms of crosslink repair are unknown. In Drosophila melanogaster, the mus308 mutation leads to marked sensitivity to DNA crosslinking agents. The C-terminal portion of the Mus308 polypeptide encodes a DNA polymerase, while a putative DNA helicase is encoded by the N-terminal portion. As a step towards isolating proteins involved in DNA crosslink repair, we searched for mammalian genes similar to the DNA helicase portion of Mus308. Human and mouse homologs were isolated from cDNA expression libraries and designated HEL308. Human HEL308 is on chromosome 4q21 and encodes a polypeptide of 1101 amino acids. The protein was expressed in insect cells and purified. HEL308 is a single-stranded DNA-dependent ATPase and DNA helicase. Mutation of a highly conserved lysine to methionine in helicase domain I eliminated both activities. The protein readily displaces 20 to 40-mer duplex oligonucleotides. Displacement of longer substrates was less efficient but was stimulated by the single-stranded DNA binding protein RPA. Activity was supported by ATP or dATP but not other nucleotide triphosphates. The enzyme translocates on DNA with 3’ to 5’ polarity, and behaves as a multimer upon gel filtration.
J. Biol. Chem, 10.1074/jbc.M110271200
Submitted on October 25, 2001
Revised on December 14, 2001
Accepted on December 18, 2001
A human DNA helicase homologous to the DNA crosslink sensitivity protein mus308
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