Thermoprotection by glycine betaine and choline

Microbiology (Reading). 1999 Sep;145 ( Pt 9):2543-2548. doi: 10.1099/00221287-145-9-2543.

Abstract

Glycine betaine is mostly known as an osmoprotectant. It is involved in the osmotic adaptation of eukaryotic and bacterial cells, and accumulates up to 1 M inside cells subjected to an osmotic upshock. Since, like other osmolytes, it can act as a protein stabilizer, its thermoprotectant properties were investigated. In vitro, like protein chaperones such as DnaK, glycine betaine and choline protect citrate synthase against thermodenaturation, and stimulate its renaturation after urea denaturation. In vivo, the internal concentration of glycine betaine is neither increased nor decreased after heat shock (this contrasts with a massive increase after osmotic upshock). However, even in exponential-phase bacteria grown in usual minimal salts media, the internal glycine betaine concentration attains levels (around 50 mM) which can protect proteins against thermodenaturation in vitro. Furthermore, glycine betaine and choline restore the viability of a dnaK deletion mutant at 42 degrees C, suggesting that glycine betaine not only acts as a thermoprotectant in vitro, but also acts as a thermoprotectant for Escherichia coli cells in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Betaine / metabolism
  • Betaine / pharmacology*
  • Choline / metabolism
  • Choline / pharmacology*
  • Citrate (si)-Synthase / chemistry
  • Citrate (si)-Synthase / metabolism
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / physiology*
  • Escherichia coli Proteins*
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism
  • Heat-Shock Response*
  • Mutation
  • Protein Folding
  • beta-Galactosidase / metabolism

Substances

  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Betaine
  • Citrate (si)-Synthase
  • beta-Galactosidase
  • dnaK protein, E coli
  • Choline