Chloroplast development requires the activities of both nuclear and chloroplast genetic systems, but the precise contribution of each and the mechanism by which they interact are not understood. A prime goal is to determine the site of synthesis of each chloroplast polypeptide. Studies with isolated subcellular systems, as well as inhibitor experiments with intact cells, have established that many chloroplast polypeptides are made by cytoplasmic ribosomes. Such polypeptides include subunits of both thylakoid and stromal multi-subunit proteins. These observations raise two questions: how do these polypeptides traverse the chloroplast envelope, and where are they assembled into whole functional proteins? The small subunit of the chloroplast enzyme ribulose biphosphate carboxylase is made in the cytoplasm as a higher molecular weight polypeptide precursor. We report here that the cleavage of this precursor and the assembly of the small subunit into whole ribulose bisphosphate carboxylase molecules takes place in the chloroplast stroma.

Item Type:	Refereed Article
Keywords:	ribulose bisphosphate carboxylase, stroma, chloroplast development
Research Division:	Biological Sciences
Research Group:	Plant Biology
Research Field:	Plant Physiology
Objective Division:	Expanding Knowledge
Objective Group:	Expanding Knowledge
Objective Field:	Expanding Knowledge in the Biological Sciences
UTAS Author:	Smith, SM (Professor Steven Smith)
ID Code:	101653
Year Published:	1979
Web of Science® Times Cited:	84
Deposited By:	Plant Science
Deposited On:	2015-06-26
Last Modified:	2015-11-16
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