Recurrent paralogy in the evolution of archaeal chaperonins

@article{Archibald1999RecurrentPI,
  title={Recurrent paralogy in the evolution of archaeal chaperonins},
  author={John M Archibald and John M. Logsdon and W. Ford Doolittle},
  journal={Current Biology},
  year={1999},
  volume={9},
  pages={1053-S6}
}
Chaperonins are multisubunit double-ring complexes that mediate the folding of nascent proteins [1] [2]. In bacteria, chaperonins are homo-oligomeric and are composed of seven-membered rings. Eukaryotic and most archaeal chaperonin rings are eight-membered and exhibit varying degrees of hetero-oligomerism [3] [4]. We have cloned and sequenced seven new genes encoding chaperonin subunits from the crenarchaeotes Sulfolobus solfataricus, S. acidocaldarius, S. shibatae and Desulfurococcus mobilis… CONTINUE READING