| Literature DB >> 572474 |
S K Jain, R K Roy, M G Pluskal, D E Croall, C Guha, S Sarkar.
Abstract
Highly purified poly(A)-containing free and polysomal mRNP particles have been isolated by chromatography of subcellular fractions of chick embryonic muscles on oligo-dT-cellulose and elution with low salt buffer at 45 degrees. The free and polysomal mRNP represent two distinct classes of macromolecules, the free particles having a more complex nucleoprotein organization than the polysomal particles. Comparison of the protein moieties of three classes of poly(A)-containing cytoplasmic mRNP -- those released from nuclei after in vitro transcription and processing (transported mRNP), the free, and polysomal mRNP -- strongly suggests that the majority of the mRNA-associated proteins are exchanged in the cytoplasm during the various functional states of mRNA. A model of translational control involving the participation of mRNA-associated proteins in chick embryonic muscles and by analogy in other differentiated eukaryotic cells is proposed.Entities:
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Year: 1979 PMID： 572474 DOI： 10.1007/bf00777492
Source DB: PubMed Journal: Mol Biol Rep ISSN： 0301-4851 Impact factor: 2.316