Abstract
Development of peptide-transport activity in the scutella of isolated barley (Hordeum vulgare l. cv. Maris Otter, Winter) embryos is shown to increase rapidly after about 15 h of imbibition, with the bulk of the transport activity being expressed by 24 h. This development is prevented by treatment of 15 h embryos with cycloheximide. Protein synthesis is found to increase in a closely related manner and also to be abolished by cycloheximide. Measurement of the incorporation of bound [35S]methionine by 15 to 21-h embryos indicates that de-novo protein synthesis during this period is greater in the scutellum than in the embryonic axis. Previous studies have shown that the peptide-transport system possesses essential dithiol groups, probably located at the substrate-binding site (Walker-Smith and Payne 1983 b, 1984b). Treatment of 15-h embryos with the non-penetrant thiol reagent p-chloromercuribenzene sulphonic acid did not affect development of peptide-transport activity during the following 6 h, whereas with 3-d embryos identical treatment inhibited uptake almost completely during a subsequent 6-h period. Radioautography revealed that amongst the proteins synthesised during this early phase of germination and labelled in vitro with [35S]methionine some are found within the epithelial plasmalemmae of the scutellum, which is the location of the peptide-transport carrier identified previously by externally labelling with a radioactive thiol reagent. The results provide evidence that protein(s) of the peptide-transport system are synthesised and inserted into the scutellum during early germination, allowing the system to play a major role in the nitrogen nutrition of the embryo.
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Abbreviations
- Gly:
-
Glycine
- Phe:
-
phenylalanine
References
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Walker-Smith, D.J., Payne, J.W. Synthesis of the peptide-transport carrier of barley scutellum during the early stages of germination. Planta 164, 550–556 (1985). https://doi.org/10.1007/BF00395974
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DOI: https://doi.org/10.1007/BF00395974