Submitted to: Gordon Research Conference Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 2/5/1999
Publication Date: N/A
Citation: N/A Interpretive Summary:
Technical Abstract: Many different environmental insults induce the stress response, including temperature extremes, pathogen attack, and exposure to toxic chemicals. In all cases, stress disrupts normal cellular protein folding. A major function of the stress response is induction of a small number of proteins that facilitate correct protein folding or re-folding. These stress proteins have been called molecular chaperones, because of their roles in preventing inappropriate interactions among different protein domains. The 70 kDa class of stress proteins comprise one major class of chaperones. Recent results have revealed that the stress proteins do not function alone within the cell but rather as components of a large chaperone hetero-complex. Eight distinct stress proteins have been identified as components of the complex isolated from cultured maize cells. A model will be presented suggesting how each of the proteins might interact with the others in promoting cellular recovery from environmental stress. Additionally, there will be comparison among bacterial, plant, and animal stress protein hetero-complexes.