Protein synthesis by isolated chloroplasts

Ellis, R. John

doi:10.1016/0304-4173(77)90008-8

Cited by 252 publications

(100 citation statements)

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“…It is concluded that cycloheximide and 2-(4-methyl-2,6-dinitroanilino)-N-methylpropionamide, under conditions which reduce small subunit synthesis by more than 90 %, , reduce the rate of synthesis of the large subunit by less than 30%. It is not possible to state whether this small effect is a direct consequence of the inhibition of cytoplasmic protein synthesis, or to side effects of these inhibitors, which have been documented for some plant tissues [25].…”

Section: Discussionmentioning

confidence: 99%

“…This interpretation is supported by three further lines of evidence. Firstly, isolated pea chloroplasts synthesize and accumulate large subunit aggregates in the absence of small subunits [6,25]. Secondly, isolated chloroplasts both elongate and initiate polypeptide chains at a significant rate [31].…”

Section: Discussionmentioning

confidence: 99%

“…The available evidence does not, however, rule out the suggestion that the small subunit, or another cytoplasmically synthesized protein, is required for the transcription of the large subunit gene [11,25]. If this is the case, a pool of such a controlling protein must exist in the cells.…”

Section: Discussionmentioning

confidence: 99%

“…Bp. C = ribulose bisphosphate carboxylase lished that this enzyme is by far the most abundant protein in leaf cells [25]. The third major band migrates with a mobility very similar to that of purified soybean chlorophyll a/b-binding protein, which is the most abundant thylakoid protein [26].…”

Section: Characterization Of Proteins Synthesized By Soybean Leuf Cellsmentioning

confidence: 99%

“…The results in Fig.9 show that even after a 2.5-h treatment with cycloheximide, newly synthesized large subunits are still being incorporated into complete ribulose bisphosphate carboxylase, under conditions in which there is no synthesis of small subunits. Blair and Ellis [6] have shown that in isolated chloroplasts (where there is no small subunit synthesis) newly synthesized large subunits migrate as aggregates on non-denaturing gels which, under certain conditions, can co-migrate with complete ribulose bisphosphate carboxylase molecules [25]. These aggregates can be separated from complete ribulose bisphosphate carboxylase molecules by electrophoresis on 4 % polyacrylamide non-denaturing gels.…”

Section: Ejject Of Cycloheximide On the Synthesis Of Complete Ribulosmentioning

confidence: 99%

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The Biosynthesis of Ribulose Bisphosphate Carboxylase

Barraclough

Ellis

1979

European Journal of Biochemistry

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Isolated leaf cells from soybean (Glycine max) incorporate [35S]methionine into protein at a linear rate for at least 5 h. Analysis of the products of incorporation by one-dimensional and two-dimensional polyacrylamide gel electrophoresis shows that major products are the large and small subunits of the chloroplast enzyme, ribulose bisphosphate carboxylase. The large subunit is synthesized by chloroplast ribosomes and the small subunit by cytoplasmic ribosomes. Addition of chloramphenicol to the cells reduces incorporation into the large subunit without affecting incorporation into the products of cytoplasmic ribosomes. Addition of cycloheximide or 2-(4-methyl-2,6-dinitroanilino)-N-methylpropionamide stops incorporation into the small subunit, but large subunit continues to be made for at least 4 h. For accurate estimates of incorporation into the large subunit, it is essential to use two-dimensional gel electrophoresis, because the large subunit region on one-dimensional gels is contaminated with the products of cytoplasmic ribosomes. Newly synthesized large subunits continue to enter complete molecules of ribulose bisphosphate carboxylase in the absence of small subunit synthesis. These results suggest that, in contrast to the situation in algal cells, the synthesis of the two subunits of ribulose bisphosphate carboxylase in the different subcellular compartments of higher plant cells is not tightly coupled over short time periods, and that a pool of small subunits exists in these cells. The results are discussed in relation to possible mechanisms for the integration of the synthesis of the large and small subunits of ribulose bisphosphate carboxylase.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Characterization Of Proteins Synthesized By Soybean Leuf Cellsmentioning

confidence: 99%

Section: Ejject Of Cycloheximide On the Synthesis Of Complete Ribulosmentioning

confidence: 99%

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