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…
1,200 Citations
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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.
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