IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock.

@article{Laskowska1996IbpAAI,
  title={IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock.},
  author={Ewa Laskowska and A Wawrzyn{\'o}w and Alan Taylor},
  journal={Biochimie},
  year={1996},
  volume={78 2},
  pages={117-22}
}
IbpA/B, 16 kDa heat-shock proteins were recently described as recognizing heterologous protein inclusion bodies in Escherichia coli cells; the corresponding genes formed an operon regulated by the rpoH gene product, sigma 32 protein (Burland et al (1993) Genomics 16, 551; Allen et al (1992) J Bacteriol 174, 6938; Chuang et al (1993) Gene 134, 1; Chuang and Blattner (1993) J Bacteriol 175, 5242). We have found that IbpA/Bs also recognize endogenous bacterial proteins aggregated intracellularly… CONTINUE READING