PMID:2897629

Citation	Hemmingsen, SM, Woolford, C, van der Vies, SM, Tilly, K, Dennis, DT, Georgopoulos, CP, Hendrix, RW and Ellis, RJ (1988) Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333:330-4
Abstract	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 'chaperonins'. Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes. Assisted post-translational assembly of oligomeric protein structures is emerging as a general cellular phenomenon.
Links	PubMed Online version:10.1038/333330a0
Keywords	Adenosine Triphosphatases/genetics; Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Chaperonin 60; Chaperonins; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Genes, Bacterial; Heat-Shock Proteins/genetics; Molecular Sequence Data; Plants/enzymology; Plants/genetics; Ribulose-Bisphosphate Carboxylase/genetics; Sequence Homology, Nucleic Acid; Species Specificity
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