The Ul snRNP-specific protein C contains an N-terminal zinc finger-ike CH motif which is required for the binding of the U1C protein to the Ul snRNP particle. Recently a similar motif was reported to be essential for in vivo homodimerization of the yeast splicing factor PRP9. In the present study we demonstrate that the human UIC protein is able to form homodimers as well. Ul C homodimers are found when (i) the human U1C protein is expressed in Escherichia coil, (ii) immunoprecipitations with anti-UI C antibodies are performed on in vitro translated Ul C, and when (iii) the yeast two hybrid system is used. Analyses of mutant Ul C proteins in an in vitro dimerization assay and the yeast two hybrid system revealed that amino acids within the CH motif, i.e. between positions 22 and 30, are required for homodimerization.
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