Microbiology · 1999 · 199 citations · 26 references
Life SciencesBiochemistryMicrobiologyMicrobial GeneticsMicrobial PhysiologyProtein FoldingHeat Stress ToleranceMolecular ChaperonesProtein MetabolismThermostable EnzymesBacterial ChaperonesCitrate SynthaseDenaturationEscherichia ColiHeat Shock ResponseOsmotic ShockOsmotic Stress AdaptationStabilization By Osmolytes
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.
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Living with Water Stress: Evolution of Osmolyte Systems
Paul H. Yancey, Mary E. Clark, Steven C. Hand et al. · Science · 1982 · 3.8K citations
The stabilization of proteins by osmolytes
Tsutomu Arakawa, Serge N. Timasheff · Biophysical Journal · 1985 · 1K citations · Full text