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Poor germination and eventual loss of viability of rye grains on storage reflects a decreasing ability of embryos to synthesize protein in vivo. Cell-free protein-synthesizing systems from low viability embryo stocks exhibit lesions in the soluble components of the post-ribosomal supernatant fractions. tRNA and aminoacyl-tRNA synthetases are not impaired. The activity of enzymes concerned with transfer of phenylalanyl-tRNA from the aminoacyl to the peptidyl site on the ribosome is slightly decreased. The transfer enzymes (transferase I) involved in the binding of phenylalanyl-tRNA to the aminoacyl site show a loss of activity that closely reflects the loss of viability and the decline of protein synthesis of the embryo in vivo. The inactivation of labile transferase I components may be a major factor leading to senescence and loss of viability in rye grains.

Protein synthesis and loss of viability in rye embryos. The lability of transferase enzymes during senescence