Translation of R17 RNA by Escherichia coli ribosomes. Initiator transfer RNA-directed binding of 30 S subunits to the starting codon of the coat protein gene.
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Biomedical subjects
Publications and source records attributed to M Noll.
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The digestion of chromatin insitu with DNase I reveals, after denaturation, a regular series of single stranded DNA fragments the lengths of which represent multiples of 10 bases. These experiments are compatible with the DNA being on the outside of the chromatin subunit and suggest that the subunit structure itself contains repetitive structural elements. Possible models are discussed.
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An initiation complex has been formed in high yields from E. coli ribosomes, 9S messenger RNA for rabbit hemoglobin, and N-formylmethionine-tRNA. Initiation factor IF-3 is required for the binding and puromycin is required for the release of fMet. Valyl-tRNA fails to bind to the second codon, whereas a mixture of 15 aminoacyl-tRNAs promotes incorporation. Together with quantitative data, the findings suggest that IF-3 directs the ribosomes to an AUG codon on one of the two globin messengers, at a site that is different from the normal starting point for globin synthesis.
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