Homologous plant and bacterial proteins chaperone oligomeric protein assembly
@article{Hemmingsen1988HomologousPA, title={Homologous plant and bacterial proteins chaperone oligomeric protein assembly}, author={Sean M. Hemmingsen and Carol A. Woolford and Saskia M. van der Vies and Kit Tilly and David T. Dennis and Costa Georgopoulos and Roger W. Hendrix and R. John Ellis}, journal={Nature}, year={1988}, volume={333}, pages={330-334} }
An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants. The product of the Escherichia coli groEL gene is essential for cell viability and is required for the assembly of bacteriophage capsids. Sequencing of the groEL gene and the complementary cDNA encoding the chloroplast protein has revealed that these proteins are evolutionary homologues which we term…
1,200 Citations
Molecular Chaperones: The Plant Connection
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- 1990
The function of chaperones forces a rethinking of the principle of protein self-assembly, and so prevents them from undergoing incorrect interactions that might produce nonfunctional structures.
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It is reported that co-expression of plant Rubisco and chaperonin genes affected the solubility and stability of Rubisco large subunit polypeptides, however, neither the assembled oligomeric protein nor Rubisco enzyme activity was detected.
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- 1989
Assembly of foreign prokaryotic ribulose bisphosphate carboxylases (Rubiscos) in Escherichia coli requires both heat-shock proteins groEL and groES. GroEL is related to a chloroplast protein…
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- 2001
The available evidence for the assembly/disassembly of type I and II chaperonins points to a process that is highly cooperative and suggests a prominent role for nucleotides, as well as a chaperone-dependent process itself and requires functional preformed chaper onin complexes.
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- 1992
Preliminary kinetic experiments are reported on that explore the interactions of cpn60 with (a) the folding intermediates of Bacillus stearothemophilus lactate dehydrogenase (LDH), (b) with ATP and an unreactive analogue (AMP-PNP), and (c) with the coprotein cpnl0.
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- 2018
Recent progress on the unique structure and function of the chloroplast chaperonin system is discussed based on model organisms Chlamydomonas reinhardtii and Arabidopsis thaliana to lead to successful reconstitution of eukaryotic Rubisco in vitro.
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It is proposed that this protein is the cytosolic chaperone involved in phytochrome biogenesis in plant cells, and can stimulate refolding of denatured phy tochrome to a photoactive form in the presence of Mg–ATP.
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