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THE PLANT CELL, Vol 1, Issue 12 1223-1230, Copyright © 1989 by American Society of Plant Biologists
Several Proteins Imported into Chloroplasts Form Stable Complexes with the GroEL-Related Chloroplast Molecular Chaperone
T. H. Lubben, G. K. Donaldson, P. V. Viitanen and A. A. Gatenby
Molecular Biology Division, Central Research and Development Department, Experimental Station, E.I. DuPont de Nemours & Co., Wilmington, Delaware 19880-0402
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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