Coilin interacts with Ku proteins and inhibits in vitro non-homologous DNA end joining.
Coilin is a nuclear protein that plays a role in Cajal body formation. The function of nucleoplasmic coilin is unknown. Here we report that coilin interacts with Ku70 and Ku80, which are major players in the DNA repair process. Ku proteins compete with SMN and SmB' proteins for coilin interaction sites. The binding domain on coilin for Ku proteins cannot be localized to one discrete region, and only full-length coilin is capable of inhibiting in vitro non-homologous DNA end joining (NHEJ). Since Ku proteins do not accumulate in CBs, these findings suggest that nucleoplasmic coilin participates in the regulation of DNA repair.
Department of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216-4505, USA.
Venkatramreddy
V
Velma
Zunamys I
ZI
Carrero
Angela M
AM
Cosman
Michael D
MD
Hebert
D001667:Binding, Competitive; D004265:DNA Helicases / Q000378:metabolism*; D004260:DNA Repair / Q000187:drug effects*; D006367:HeLa Cells; D006801:Humans; D000072200:Ku Autoantigen; D009687:Nuclear Proteins / Q000378:metabolism* / Q000494:pharmacology*; D011995:Recombination, Genetic / Q000187:drug effects*; D055533:Survival of Motor Neuron 1 Protein / Q000378:metabolism; D055517:snRNP Core Proteins / Q000378:metabolism
D009687:Nuclear Proteins; C526407:SNRPB protein, human; D055533:Survival of Motor Neuron 1 Protein; D055517:snRNP Core Proteins; C068921:p80-coilin; D004265:DNA Helicases; C106893:XRCC5 protein, human; D000072200:Ku Autoantigen