JBC INTERFERin siRNA transfection reagent

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The Interaction of Aminoacyl Soluble Ribonucleic Acid and Aminoacyl Transferase I

Fumio Ibuki 1, Eugeniusz Gasior 1, and Kivie Moldave 1

From the 1 From the Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111

Incubation of one of the aminoacyl-transferring factors, transferase I, at 37° leads to its rapid and irreversible loss of activity. This enzyme is protected against loss of activity by aminoacyl soluble ribonucleic acid (sRNA) but not by stripped sRNA, synthetic polynucleotides, ribosomes, transferase II, guanosine triphosphate, or sulfhydryl compounds. Protection is highly dependent on the presence of sRNA-bound amino acids but is not specific for a particular amino acid. The rate of hydrolysis of aminoacyl-sRNA is significantly slower in the presence of transferase I; ribosomes, transferase II, and other components of the aminoacyl transfer reaction do not affect the rate of deacylation. These results suggest that the interaction of aminoacyl-sRNA and transferase I yields a product in which both components are more stable than either one in the free form. The high degree of specificity for aminoacyl-sRNA and transferase I in this interaction may reflect an intermediary stage in polypeptide biosynthesis, between aminoacyl-sRNA and ribosome-bound aminoacyl-sRNA or peptidyl-sRNA.

Submitted on December 6, 1965


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