Abstract
Messenger ribonucleoproteins, first discovered in our laboratory (1964) as mRNA-containing particles of fish embryo cytoplasm and named informosomes, were later found to be universally occurred in eukaryotic cells. Messenger ribonucleoproteins of different intracellular localization such as free cytoplasmic informosomes, translatable messenger ribonucleoproteins in polyribosomes (“polyribosomal informosomes”) and nuclear pre-mRNA-containing particles (“nuclear informosomes”) are characterized by a number of features common for all of them. However, the transport from the nucleus into the cytoplasm as well as the transition from the free non-translatable state into the polyribosome-bound translatable state are accompanied by essential changes in the protein moiety of the particles.
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