Heat shock proteins: molecular chaperones of protein biogenesis.

摘要: Heat shock proteins (Hsps) were first identified as whose synthesis was enhanced by stresses such an increase in temperature. Recently, several of the major Hsps have been shown to be intimately involved protein biogenesis through a direct interaction with wide variety proteins. As reflection this role, these referred molecular chaperones. Hsp70s interact incompletely folded proteins, nascent chains on ribosomes and process translocation from cytosol into mitochondria endoplasmic reticulum. Hsp60 also binds unfolded preventing aggregation facilitating folding. Although less well defined, other Hsp90 play important roles modulating activity number The function proteolytic system is intertwined that Several components system, encoded heat-inducible genes, are responsible for degradation abnormal or misfolded budding yeast Saccharomyces cerevisiae has proven very useful analysis role chaperones maturation, translocation, degradation. In review, results experiments discussed within context organisms attempt describe current state understanding ubiquitous