Chaperonins dependent increase of Cu,Zn superoxide dismutase production in Escherichia coli

FEBS Lett. 1993 May 3;322(1):6-9. doi: 10.1016/0014-5793(93)81099-l.

Abstract

Over-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-dependent pattern of expression of Cu,Zn superoxide dismutases in Escherichia coli and increased the yield of active enzyme. The results obtained indicate that chaperonins prevent degradation of metal-deficient enzyme molecules. GroEL was shown to form a complex with unfolded Cu,Zn superoxide dismutase in vitro, confirming that GroEL can interact with beta-stranded proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Cattle
  • Chaperonin 10
  • Chaperonin 60
  • Chaperonins
  • Escherichia coli / enzymology*
  • Gene Expression
  • Heat-Shock Proteins / metabolism
  • Humans
  • Metals / metabolism
  • Proteins / metabolism*
  • Superoxide Dismutase / biosynthesis*
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism
  • Xenopus laevis

Substances

  • Bacterial Proteins
  • Chaperonin 10
  • Chaperonin 60
  • Heat-Shock Proteins
  • Metals
  • Proteins
  • Superoxide Dismutase
  • Chaperonins