Abstract
f2 RNA in which all exposed, unpaired cytosines are modified with methoxyamine retains an unchanged ordered structure. This RNA shows the same capacity to direct fMet-tRNA binding to E. coli ribosomes as unmodified f2 RNA. As this binding corresponds mainly to the coat protein initiation site, our results suggest that unpaired cytosines present in the coat protein initiation fragment are not involved in the specific recognition of that fragment by ribosomes. When f2 RNA is treated with methoxyamine in the presence of guanidine-HCl the resulting modified f2 RNA becomes irreversibly unfolded. Such RNA stimulates fMet-tRNA binding about 50 times more efficiently than native f2 RNA. E. coli ribosomal RNA when unfolded under the same conditions also stimulates very efficiently the binding of fMet-tRNA.
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