Homologous plant and bacterial proteins chaperone oligomeric protein assembly
- 1 May 1988
- journal article
- Published by Springer Nature in Nature
- Vol. 333 (6171), 330-334
- https://doi.org/10.1038/333330a0
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.This publication has 44 references indexed in Scilit:
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