Abstract
The proteins associated with poly(A) and other regions of mRNA and hnRNA molecules in mouse L cells were investigated with the aid of ultraviolet light-induced crosslinking of proteins to RNA. The poly(A)s of polyribosomal and free cytoplasmic mRNAs are associated with a protein, p78A. In contrast, the poly(A) of hnRNA is associated with a smaller protein, p60A, that differs from p78A in its partial peptide map. p78A occurs free in the cytoplasm, but p60A does not. There is a second 78 kd protein, p78X, associated with mRNA sequences other than poly(A). p78X differs from p78A in its partial peptide map. The total proteins crosslinked to polyribosomal and free cytoplasmic mRNAs are similar. However, the total proteins crosslinked to hnRNA are quite different from those crosslinked to mRNA. We suggest that newly synthesized mRNA molecules emerging from the nucleus into the cytoplasm shed the proteins with which they were associated in the nucleus and become associated with a new set of proteins derived from the cytosol. Furthermore, the cytoplasmic mRNA-associated proteins continue to exchange with free proteins.
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