Identification and Origin of Some Chloroplast Aminoacyl-tRNA Synthetases and tRNAs

Bonnie J. Reger, S. A. Fairfield, J.L. Epler, W. Edgar Barnett

Proceedings of the National Academy of Sciences · 1970 · 74 citations · 9 references

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Abstract

Light-grown, wild type Euglena gracilis contains two aminoacyl-tRNA synthetases for both phenylalanine and isoleucine. Only one of the two synthetases for each amino acid is found in isolated chloroplasts, as are the light-induced phenylalanine and isoleucine tRNAs. In each case the light-induced chloroplast tRNAs can only be acylated by the chloroplast synthetases. The chloroplast isoleucyl-tRNA synthetase is light-inducible and cannot be detected in dark-grown cells or in cells of the bleached mutant W(3)BUL. The presence of the chloroplast phenylalanyl-tRNA synthetase in W(3)BUL, which contains no chloroplast DNA or structure, indicates that this chloroplast enzyme is synthesized in the cytoplasm and is coded by nuclear genes.

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