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The synthesis and deposition of the prolamin storage proteins (secalins) of rye



The synthesis and deposition of the prolamin storage proteins (secalins) of rye



Planta 159(5): 439-445



The synthesis and deposition of the endosperm storage proteins of rye, usually termed secalins, was studied. The rate of accumulation of secalin in developing rye grain was highest 3-5 wk after anthesis. Some changes in the proportions of the 4 major groups of secalin polypeptides were observed during maturation, notably an increase in gamma -secalins of mol. wt. 75 000 and a decrease in omega -secalins. In vitro translation of mRNA fractions prepared from 4-wk-old endosperms showed that secalin polypeptides were synthesised on membrane-bound polysomes. The secalin products were identified by their mobilities on sodium dodecylsulphate-polyacrylamide gel electrophoresis and their relative incorporation of radioactive lysine, glycine, proline, leucine and methionine. Protein bodies prepared by sucrose density ultracentrifugation contained reduced amounts of gamma -secalins of mol. wt. 40 000 and omega -secalins compared with the total secalin fraction, but these components were present in the expected amounts when 1M NaCl was added to the buffers. Treatment of the protein bodies with proteinase-k resulted in the digestion of their contents regardless of the presence of NaCl, indicating that the surrounding membrane was incomplete. It was concluded that the NaCl reduced the loss of secalins from the protein bodies by decreasing secalin solubility rather than by affecting the integrity of the protein body membrane. The results reported for the synthesis and deposition of secalins are consistent with the results of previous studies on the prolamins of wheat and barley.

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Accession: 001272428

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PMID: 24258297

DOI: 10.1007/bf00392080


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