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- W2079380272 abstract "The role of proteins bound to mRNA is one of the key problems in the study of polysomal messenger ribonucleoprotein complexes. In this paper it is shown that the use of ethylenediamine tetraacetic (EDTA) should be avoided during the purification of the mRNA · protein complexes. The property of cultured cells to release mRNA from polysomes at high temperature (43°C) was used to purify polysomal messenger ribonucleoprotein complexes. The polysomal messenger ribonucleoprotein complexes so obtained bind to salt washed ribosomes even at 0°C. Under the same conditions naked mRNA does not bind to ribosomes. These experiments indicate that certain proteins attached to mRNA are essential for its activity. The polysomal messenger ribonucleoprotein complexes are bound to the small subunits and their mRNA is partially protected by the ribosomes. This association is not an artificial aggregation. The study of the complexes reveals that neither poly(A) sequences nor double-stranded regions of the mRNA, but a protein of the polysomal messenger ribonucleoprotein complexes are involved in the binding. The described polysomal messenger ribonucleoprotein · ribosome complex does not represent a complete initiation complex because some initiation factors are absent and must be added to assure protein synthesis." @default.
- W2079380272 created "2016-06-24" @default.
- W2079380272 creator A5040819874 @default.
- W2079380272 date "1977-06-01" @default.
- W2079380272 modified "2023-09-25" @default.
- W2079380272 title "Proteins of the polysomal messenger ribonucleoprotein are responsible for its association with the 40-S ribosomal subunit in HeLa cells" @default.
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- W2079380272 doi "https://doi.org/10.1016/0005-2787(77)90007-7" @default.
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