Effects of recombinant protein misfolding and aggregation on bacterial membranes.

@article{Ami2009EffectsOR,
  title={Effects of recombinant protein misfolding and aggregation on bacterial membranes.},
  author={Diletta Ami and Antonino Natalello and Tina Schultz and Pietro Gatti-Lafranconi and Marina Lotti and Silvia Maria Doglia and Antonio De Marco},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1794 2},
  pages={263-9}
}
The expression of recombinant proteins is known to induce a metabolic rearrangement in the host cell. We used aggregation-sensitive model systems to study the effects elicited in Escherichia coli cells by the aggregation of recombinant glutathione-S-transferase and its fusion with the green fluorescent protein that, according to the expression conditions, accumulate intracellularly as soluble protein, or soluble and insoluble aggregates. We show that the folding state of the recombinant protein… CONTINUE READING