The discovery of chaperonins

@article{Smith1999TheDO,
  title={The discovery of chaperonins},
  author={Tracy Smith},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={1090-1090},
  url={https://api.semanticscholar.org/CorpusID:6158370}
}
  • Tracy Smith
  • Published in Nature Structural Biology 1 December 1999
  • Biology, Chemistry, Materials Science
  • Nature Structural Biology
View on Nature
nature.com

7 References

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.

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

It is proposed that mitochondrial heat-shock protein hsp60 catalyses protein folding in an ATP-mediated reaction, followed by release of the bound polypeptides.

Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

The cloning and characterization of a nuclear gene is reported, HSP60, which codes for the hsp60 homologue from the yeast Saccharomyces cerevisiae, which was found to be the genetic locus of the conditional-lethal mutation described by Cheng et al.8, which at non-permissive temperature is defective in the assembly of several different multisubunit complexes in mitochondria.

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

A nuclear encoded mitochondrial heat-shock protein hsp60 is required for the assembly into oligomeric complexes of proteins imported into the mitochondrial matrix. hsp60 is a member of the…

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes and are implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants.

Host participation in bacteriophage lambda head assembly.

Properties of a mutant of Escherichia coli defective in bacteriophage λ head formation (groE)

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