Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins.
AUTOR(ES)
Minton, K W
RESUMO
It is demonstrated experimentally that addition of proteins that are themselves resistant to denaturation by heat or ethanol can nonspecifically stabilize other proteins that are ordinarily highly susceptible to inactivation. It is proposed that the diffusion-limited rate with which unfolded protein molecules encounter each other and become irreversibly crosslinked is reduced in the presence of substantial concentrations of an unreactive globular protein. We suggest that one of the functions of heat shock proteins, which are synthesized in large amounts after exposure of cells to increased temperature and other forms of stress, may be to stabilize other proteins kinetically in a similarly nonspecific fashion.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=347287Documentos Relacionados
- Heat shock proteins: regulators of stress response and apoptosis
- Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins.
- Self-degradation of heat shock proteins.
- Newcastle disease virus stimulates the cellular accumulation of stress (heat shock) mRNAs and proteins.
- Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins.
