Bacterial inclusion bodies are cytotoxic in vivo in absence of functional chaperones DnaK or GroEL.
Cytotoxicity of cytoplasmic bacterial inclusion bodies has been explored in vivo in cells producing a model, misfolding-prone beta-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.
González-Montalbán
Nuria
N
Institut de Biotecnologia i de Biomedicina, Departament de Genètica i de Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain.
Carrió
M Mar
MM
Cuatrecasas
Sergi
S
Arís
Anna
A
Villaverde
Antonio
A
D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism*; D049071:Endopeptidase Clp / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000254:growth & development*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D002479:Inclusion Bodies / Q000235:genetics / Q000378:metabolism*; D049070:Protease La / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism*
D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D011993:Recombinant Fusion Proteins; D001616:beta-Galactosidase; C483568:ClpA protease, E coli; C483567:Lon protein, E coli; D049070:Protease La; D049071:Endopeptidase Clp; C063842:dnaK protein, E coli