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… 
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Highly Influential Citations
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Background Citations
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Methods Citations
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1,204 Citations

The complexity of chloroplast chaperonins.
Molecular Chaperones: The Plant Connection
TLDR
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.
Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli
TLDR
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.
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
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…
Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.
TLDR
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.
Assembly of chaperonin complexes
TLDR
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.
The Influence of Chaperonins on Protein Folding
TLDR
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.
Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis
TLDR
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.
3 – Chaperonins of Photosynthetic Organisms
ATCPl-related molecular chaperone from plants refolds phytochrome to its photoreversible form
TLDR
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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References

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TLDR
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TLDR
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TLDR
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  • J. Bardwell, E. Craig
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1987
TLDR
The isolation of an E. coli homologue of hsp83 illustrates the remarkable conservation of heat shock proteins in evolution and will facilitate genetic and biochemical experiments aimed at determining the function of hSp83.
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TLDR
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High molecular weight pea leaf protein similar to the groE protein of escherichia coli
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