A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1

@article{Trent1991AMC,
  title={A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1},
  author={Jonathan D. Trent and Elmar Nimmesgern and Joseph S. Wall and F. Ulrich Hartl and Arthur L Horwich},
  journal={Nature},
  year={1991},
  volume={354},
  pages={490-493}
}
THERE is evidence to suggest that components of archaebacteria are evolutionarily related to cognates in the eukaryotic cytosol–7. We postulated that the major heat-shock protein of the thermophilic archaebacterium, Sulfolobus shibatae, is a molecular chaperone and that it is related to an as-yet unidentified chaperone component in the eukaryotic cytosol. Acquired thermotolerance in S. shibatae correlates with the predominant synthesis of this already abundant protein, referred to as… CONTINUE READING