Bacterial inclusion bodies are cytotoxic in vivo in absence of functional chaperones DnaK or GroEL

• Published in: Journal of biotechnology 2005-09, Vol.118 (4), p.406-412
• Main Authors: González-Montalbán, Nuria, Carrió, M. Mar, Cuatrecasas, Sergi, Arís, Anna, Villaverde, Antonio
• Format: Article
• Language: English
• Subjects: Aggregation; beta-Galactosidase - genetics; beta-Galactosidase - metabolism; Biological and medical sciences; Biotechnology; Chaperones; Chaperonin 60 - genetics; Chaperonin 60 - metabolism; DnaK; E. coli; Endopeptidase Clp - genetics; Endopeptidase Clp - metabolism; Escherichia coli; Escherichia coli - growth & development; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Fundamental and applied biological sciences. Psychology; GroEL; HSP70 Heat-Shock Proteins - genetics; HSP70 Heat-Shock Proteins - metabolism; Inclusion Bodies - genetics; Inclusion Bodies - metabolism; Protease La - genetics; Protease La - metabolism; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism
• ISSN: 0168-1656; 1873-4863
• DOI: 10.1016/j.jbiotec.2005.05.024

Cytotoxicity of cytoplasmic bacterial inclusion bodies has been explored in vivo in cells producing a model, misfolding-prone β-galactosidase fusion protein. The formation of such aggregates does not result in detectable toxicity on Escherichia coli producing cells. However, a deficiency in the main chaperones DnaK or GroEL but not in other components of the heat shock system such as the chaperone ClpA or the protease Lon, promotes a dramatic inhibition of cell growth. The role of DnaK and GroEL in minimizing toxicity of in vivo protein aggregation is discussed in the context of the conformational stress and the protein quality control system.