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

Nuria González-Montalbán, M. Mar Carrió, Sergi Cuatrecasas, Anna Arís, Antonio Villaverde

Research output: Contribution to journalArticleResearchpeer-review

23 Citations (Scopus)

Abstract

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. © 2005 Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)406-412
JournalJournal of Biotechnology
Volume118
Issue number4
DOIs
Publication statusPublished - 10 Sep 2005

Keywords

  • Aggregation
  • Chaperones
  • DnaK
  • E. coli
  • GroEL
  • Protein folding

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