THE EFFECT OF ENZYMATICALLY SYNTHESIZED RIBONUCLEIC ACID ON AMINO ACID INCORPORATION BY A SOLUBLE PROTEIN-RIBOSOME SYSTEM FROM ESCHERICHIA COLI

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Abstract
Amino-acid incorporation was studied in a partially resolved E. coli extract from which the bulk of DNA was removed. Incorporation was dependent on ribosomal and soluble protein fractions, ATP and Mg++. It is stimulated by a mixture of amino-acids, KC1, amino-acid acceptor RNA and GTP (guanidine triphosphate) this combined group is referred to as the soluble protein-ribosome system. Incorporation in this sytem is blocked by RNase or chloramphenicol, but it is not affected by DNase. Addition of purified E. coli RNA polymerase has no effect on amino-acid incorporation; however, addition of T2, T4 or T6 phage DNA results in an increase of 4-fold in rate and up to 20-fold in extent of the reaction. DNase used with this is strongly inhibitory. The extent of amino-acid incorporation in the soluble protein-ribosome system can be increased 3- to 5-fold by the addition of enzymatically synthesized RNA in the absence of RNA polymerase and DNA. This increase is not affected by DNase.