Homologous plant and bacterial proteins chaperone oligomeric protein assembly

  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},
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… 
Molecular Chaperones: The Plant Connection
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
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.
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
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
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
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.
ATCPl-related molecular chaperone from plants refolds phytochrome to its photoreversible form
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.


Expression of Cyanobacterial and Higher-Plant Ribulose 1,5-Bisphosphate Carboxylase Genes in Escherichia coli
The assembly of functional RuBP carboxylase in E. coli cells containing L subunits with an M13 phage expressing the cyanobacterial S gene demonstrates the essential role of the S subunit in allowing the formation of an active enzyme.
Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits.
The ribulosebisphosphate-carboxylase large-subunit binding protein from Pisum sativum chloroplasts is an oligomer of two types of subunit with the composition alpha 6 beta 6. These two subunits are
Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein.
The previously reported dissociation of the binding protein-large subunit complex upon addition of ATP in vitro has been confirmed and the fates of the dissociated subunits further investigated.
The Rubisco large subunit binding protein
Newly synthesized Rubisco large subunits made by isolated intact chloroplasts from Pisum sativum are bound non-covalently to another protein, termed the Rubisco large subunit binding protein. This
A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.
It is shown that a Tetrahymena thermophila 58-kilodalton mitochondrial protein (hsp58) displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae, Xenopus laevis, Zea mays, and human cells, and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes.
Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.
  • J. Bardwell, E. Craig
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1987
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.
Inhibition of ribulose bisphosphate carboxylase assembly by antibody to a binding protein
It appears that all assembly-competent large subunits are associated with the binding protein, either in the 7S complex or in the 29S complex, which may represent the first example of non-autonomous protein assembly in higher plants and may pose problems for the genetic engineering of RuBisCO from these organisms.