Polypeptides of nonpolyribosomal messenger ribonucleoprotein complexes of sea urchin eggs

RNA competent in directing protein synthesis is sequestered in unfertilized sea urchin eggs as translationally quiescent, nonpolyribosomal, messenger ribonucleoprotein complexes (mRNPs). Following fertilization, these mRNPs are derepressed and actively translated, presumably due to changes in the mRNA-associated proteins and their interaction with the mRNA. We have isolated poly(A)-containing egg mRNPs free of contaminating monoribosomes and ribosomal subunits by chromatography on oligo(dT)-cellulose and identified their constituent proteins. Egg mRNPs isolated by using near physiological ionic conditions have 15-20 major proteins, most of which are in the molecular weight range of 40 000-100 000, and approximately 15-23 minor proteins in the 22 000-190 000 molecular range. The association of the proteins with poly(A)-containing mRNA is indicated by their greatly reduced retention on oligo(dT)-cellulose after pretreatment of the crude mRNP fraction with saturating amounts of poly(uridylic acid). Three of the proteins present in poly(A)-containing mRNPs from eggs, with molecular weights of 48 000, 67 000, and 140 000, were not detected in poly(A)-containing mRNPs derived from polyribosomes of hatched blastula-stage embryos. In addition, stoichiometric differences were found between some of the proteins associated with the two types of mRNP. The potential regulatory role of these proteins is discussed.