Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone. (original) (raw)

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Molecular Biology Division, E.I. DuPont de Nemours & Co., Wilmington, Delaware 19880-0402.

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Molecular Biology Division, E.I. DuPont de Nemours & Co., Wilmington, Delaware 19880-0402.

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Molecular Biology Division, E.I. DuPont de Nemours & Co., Wilmington, Delaware 19880-0402.

Search for other works by this author on:

Molecular Biology Division, E.I. DuPont de Nemours & Co., Wilmington, Delaware 19880-0402.

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Published:

01 December 1989

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T H Lubben, G K Donaldson, P V Viitanen, A A Gatenby, Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone., The Plant Cell, Volume 1, Issue 12, December 1989, Pages 1223–1230, https://doi.org/10.1105/tpc.1.12.1223
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Abstract

Nine different proteins were imported into isolated pea chloroplasts in vitro. For seven of these [the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), beta-subunit of ATP synthase, glutamine synthetase, the light-harvesting chlorophyll a/b binding protein, chloramphenicol acetyltransferase, and pre-beta-lactamase], a fraction was found to migrate as a stable high-molecular-weight complex during nondenaturing gel electrophoresis. This complex contained the mature forms of the imported proteins and the groEL-related chloroplast chaperonin 60 (previously known as Rubisco subunit binding protein). Thus, the stable association of imported proteins with this molecular chaperone is widespread and not necessarily restricted to Rubisco subunits or to chloroplast proteins. With two of the imported proteins (ferredoxin and superoxide dismutase), such complexes were not observed. It seems likely that, in addition to its proposed role in assembly of Rubisco, the chloroplast chaperonin 60 is involved in the assembly or folding of a wide range of proteins in chloroplasts.

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© 1989 by American Society of Plant Biologists

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