Abstract
The co-purification of the U1snRNP particle with a high-molecular-weight human homologous pairing activity has been observed consistently. Using human autoimmune sera directed against various snRNPs, it has been found that autoantibody binding to antigenic determinants specifically associated with the U1snRNP particle inhibits the formation of paired DNA molecules by the human homologous pairing activity. Immunoprecipitation of U1snRNP with anti-(U1)RNP autoantibodies significantly reduced the homologous pairing activity in these fractions. NaDodSO4-PAGE analysis of immunoprecipitated samples has revealed their content to be mostly composed of anti-(U1)RNP precipitable material. Taken together, these results suggest that some biochemical reactions in the process of homologous pairing promoted by high-molecular-weight complex are dependent upon U1snRNP components. It is postulated that the U1snRNP may be associated with the recombination complex in human cells.
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