Missiakas D, Raina S
Centre National de Recherche Scientifique LIDSM, Marseille, France.
Trends Biochem Sci. 1997 Feb;22(2):59-63. doi: 10.1016/s0968-0004(96)10072-4.
Depending on their cellular localization, misfolded proteins in Escherichia coli trigger two different heat-shock responses. Cytoplasmic proteins induce the 'classical' heat-shock regulon transcribed by the E sigma 32 polymerase. By contrast, misfolding of proteins in the cell envelope induces the newly described E sigma E-dependent regulon. This implies that there is an inducible transduction machinery in the inner membrane. The response to protein misfolding in the cell envelope is a finely tuned system regulated by a cascade of phosphorylation and dephosphorylation reactions.
根据其细胞定位，大肠杆菌中错误折叠的蛋白质会引发两种不同的热休克反应。细胞质中的蛋白质会诱导由E σ32聚合酶转录的“经典”热休克调节子。相比之下，细胞膜中蛋白质的错误折叠会诱导新描述的依赖E σE的调节子。这意味着在内膜中存在一种可诱导的转导机制。对细胞膜中蛋白质错误折叠的反应是一个由一系列磷酸化和去磷酸化反应调节的精细系统。
