Protein aggregation in Escherichia coli: Role of proteases

Ran Rosen, Dvora Biran, Eyal Gur, Dörte Becher, Michael Hecker, Eliora Z. Ron

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

Abstract

Protein aggregation is involved in several human diseases, and presumed to be an important process in protein quality control. In bacteria, aggregation of proteins occurs during stress conditions, such as heat shock. We studied the protein aggregates of Escherichia coli during heat shock. Our results demonstrate that the concentration and diversity of proteins in the aggregates depend on the availability of proteases. Aggregates obtained from mutants in the Lon (La) protease contain three times more protein than wild-type aggregates and show the broadest protein diversity. The results support the assumption that protein aggregates are formed from partially unfolded proteins that were not refolded by chaperones or degraded by proteases.

Original languageEnglish
Pages (from-to)9-12
Number of pages4
JournalFEMS Microbiology Letters
Volume207
Issue number1
DOIs
StatePublished - 22 Jan 2002
Externally publishedYes

Keywords

  • ClpP protease
  • Heat shock
  • HslVU protease
  • Lon (La) protease

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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