JBC, Vol. 252, Issue 4, 1156-1161, Feb, 1977
Properties of a nuclear polyadenylate-protein complex from mouse ascites cells
T. J. Quinlan, A. J. Kinniburgh and T. E. Martin
Ribonucleoprotein (RNP) subcomplexes containing at least 60% of the total
nuclear poly(A) were isolated from mouse ascites cells; these 15 S
ribonucleoprotein particles were most probably derived from larger hnRNA
containing complexes. The buoyant density of the 15 S ribonucleoprotein in
formaldehyde-CsCl was significantly less than that of the hnRNA-containing
30 S ribonucleoprotein subcomplex, indicating a higher proportion of
protein (approximately 80%) in the 15 S ribonucleoprotein. The proteins
partially protected the poly(A) from the action of ribonuclease T2. RNA
isolated from purified 15 S ribonucleoprotein was estimated to be 190 to
200 nucleotides in length by gel electrophoresis, whereas the RNA from
crude preparations was slightly larger. Base composition analysis of
32P-labeled crude 15 S RNP-RNA showed it to be rich in adenylate (70%) but
containing a substantial amount of uridylate (20%). The base composition of
RNA from purified complexes was approximately 90% adenyalte. Our results
suggested that oligo(U) sequences from hnRNA could artificially associated
with the poly(A) during preparation of 15 S RNP-RNA.