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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.
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Cold Spring Harb Symp Quant BiolHome page
T. Martin, P. Billings, J. Pullman, B. Stevens, and A. Kinniburgh
Substructure of Nuclear Ribonucleoprotein Complexes
Cold Spring Harb Symp Quant Biol, January 1, 1978; 42(0): 899 - 909.
[Abstract] [PDF]




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