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do.Sequence-specific interactionof the RNA recognition motif ofhuman Ku80 with a conserved mRNA
3' end. Ku, an essential protein
involved in trans-somal and transnuclear DNA repair, is a highmolecular weight DNA- and RNAbinding protein that requires anRNA binding motif (RBM) in its
amino-terminal domain forfunctional activity. Here, wereport the identification of anovel RBM at the amino-terminal
amino acid 198 of human Ku80.
Mutating the conserved arginine
in this RBM to alanine (RBMm)
abolished both homo- andheterodimerization of Ku80 withKu70 and Ku86. Mapping of thesequence requirement for specificbinding of Ku80 to target RNA

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revealed a specific hybridizationsite at the 5' splice site of thepre-mRNA. Mutating thishybridization site abolished Ku80
homo-dimerization. Interestingly,
this sequence is absent from the3' splice site and its mutation
did not affectheterodimerization. Hybridizationof the nucleoprotein of Ku80 RBMm
with a 4-base-long ssRNA wasreduced significantly.Q: How to
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