Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies

Andrea Vera, Anna Arís, Mar Carrió, Nuria González-Montalbán, Antonio Villaverde

Research output: Contribution to journalArticleResearchpeer-review

25 Citations (Scopus)

Abstract

Aggregated protein is solubilized by the combined activity of chaperones ClpB, DnaK and small heat-shock proteins, and this could account, at least partially, for the physiological disintegration of bacterial inclusion bodies. In vivo, the involvement of proteases in this process had been suspected but not investigated. By using an aggregation prone β-galactosidase fusion protein produced in Escherichia coli, we show in this study that the main ATP-dependent proteases Lon and ClpP participate in the physiological disintegration of cytoplasmic inclusion bodies, their absence minimizing the protein removal up to 40%. However, the role of these proteases is clearly distinguishable especially regarding the fate of solubilized protein. While Lon appears as a minor contributor in the disintegration process, ClpP directs an important attack on the released or releasable protein even not being irreversibly misfolded. ClpP is then observed as a wide-spectrum, main processor of aggregation-prone proteins and also of polypeptides physiologically released from inclusion bodies, even when occurring as soluble versions with a conformation compatible with their enzymatic activity. © 2005 Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)163-171
JournalJournal of Biotechnology
Volume119
Issue number2
DOIs
Publication statusPublished - 23 Sep 2005

Keywords

  • Aggregation
  • E. coli
  • Inclusion bodies
  • Protein folding
  • Proteolysis

Fingerprint Dive into the research topics of 'Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies'. Together they form a unique fingerprint.

Cite this