Abstract
Chloroplasts isolated fromSorghum vulgare are active in light-dependent, organelle protein synthesis. Intact chloroplasts can use light as an energy source; photosynthetically inactive chloroplasts require the addition of ATP for this protein synthesis. Preincubation of chloroplasts in light at 25°C for 1 h depleted the endogenous templates completely; such preincubated chloroplasts translated exogenously added heterologous templates efficiently. When total cellular RNA fromChlorella protothecoides, a C3 plant, was used as template for translation in a cell-free light-dependent system of isolated mesophyll chloroplasts fromSorghum vulgare, a C4 type plant, polypeptides of 55 kDa (large subunit) and 15 kDa (small subunit) were detectable in the fluorographic profile of the newly synthesized proteins; these polypeptides were absent in the products obtained with endogenous RNA. Evidence for the fidelity of the system was obtained by immunological analysis of ribulose 1, 5-bisphosphate carboxylase obtained by the translation ofChlorella cellular RNAs.
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Abbreviations
- RuBP:
-
Ribulose 1, 5-bisphosphate
- Mr :
-
relative molecular mass
- LSU:
-
large subunit
- SSU:
-
small subunit
- TCA:
-
trichloro acetic acid
- SDS:
-
sodium dodecyl sulphate
- PAGE:
-
polyacrylamide gel electrophoresis
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Valliammai, T., Krishnasamy, S. & Gnanam, A. Synthesis of ribulose 1,5-bisphosphate carboxylase by isolatedSorghum mesophyll chloroplasts. J Biosci 13, 21–32 (1988). https://doi.org/10.1007/BF02832208
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DOI: https://doi.org/10.1007/BF02832208