Small nuclear RNA-protein complex anchors on the actin filaments in bovine lymphocyte nuclear matrix.

When the nuclear matrix from bovine lymphocytes was digested by RNase-depleted trypsin, the bulk of the matrix proteins, except actin, were hydrolyzed. The digestion left rapidly sedimented spherical structures (trypsin-treated nuclear matrix), which mainly were composed of actin (Nakayasu, H. and K. Ueda. Exp. Cell Res. 143, 55-62, 1983). Almost all the small nuclear RNAs of the original nuclear matrix remained associated with these actin spheres after trypsin digestion. By sonication, the small nuclear RNPs (snRNPs) in both untreated and trypsin-treated nuclear matrices were solubilized in association with proteinous filaments of various size. The sedimentation pattern of these snRNP complexes was not changed by the digestion of the bulk of the proteins. The snRNP complex was adsorbed on rabbit muscle myosin-Sepharose then eluted by the addition of 5 mM ATP. We concluded that snRNPs are associated with actin filaments in the nuclear matrix of bovine lymphocytes.