Homologous plant and bacterial proteins chaperone oligomeric protein assembly
SM Hemmingsen, C Woolford, SM van der Vies, K Tilly… - Nature, 1988 - nature.com
SM Hemmingsen, C Woolford, SM van der Vies, K Tilly, DT Dennis, CP Georgopoulos…
Nature, 1988•nature.comAn 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 …
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 …
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.
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