Glutamate optimizes enzymatic activity under high hydrostatic pressure in Desulfovibrio species: effects on the ubiquitous thioredoxin system - Archive ouverte HAL Access content directly
Journal Articles Extremophiles Year : 2021

Glutamate optimizes enzymatic activity under high hydrostatic pressure in Desulfovibrio species: effects on the ubiquitous thioredoxin system

Hélène Gaussier
Edwige Garcin
  • Function : Author
Olivier Bornet
  • Function : Author
  • PersonId : 1075953
Marc Garel
Christian Tamburini
Laetitia Pieulle
  • Function : Author
  • PersonId : 1021199
Alain Dolla
Nathalie Pradel

Abstract

In piezophilic microorganisms, enzymes are optimized to perform under high hydrostatic pressure. The two major reported mechanisms responsible for such adaptation in bacterial species are changes in amino acids in the protein structure, favoring their activity and stability under high-pressure conditions, and the possible accumulation of micromolecular co-solutes in the cytoplasm. Recently, the accumulation of glutamate in the cytoplasm of piezophilic Desulfovibrio species has been reported under high pressure growth conditions. In this study, analysis of the effect of glutamate on the enzymatic activity of the thioredoxin reductase/thioredoxin enzymatic complex of either a piezosensitive or a piezophilic microorganism confirms its role as a protective co-solute. Analysis of the thioredoxin structures suggests an adaptation both to the presence of glutamate and to high hydrostatic pressure in the enzyme from the piezophilic strain. Indeed, the presence of large surface pockets could counterbalance the overall compression that occurs at high hydrostatic pressure to maintain enzymatic activity. A lower isoelectric point and a greater dipolar moment than that of thioredoxin from the piezosensitive strain would allow the protein from the piezophilic strain to compensate for the presence of the charged amino acid glutamate to interact with its partner.
Fichier principal
Vignette du fichier
version accepte-hal.pdf (741.69 Ko) Télécharger le fichier
Origin : Files produced by the author(s)

Dates and versions

hal-03272295 , version 1 (28-06-2021)

Identifiers

Cite

Hélène Gaussier, M. Nouailler, Edouard Champaud, Edwige Garcin, Sebban -Kreuzer, et al.. Glutamate optimizes enzymatic activity under high hydrostatic pressure in Desulfovibrio species: effects on the ubiquitous thioredoxin system. Extremophiles, 2021, 25, pp.385-392. ⟨10.1007/s00792-021-01236-x⟩. ⟨hal-03272295⟩
118 View
172 Download

Altmetric

Share

Gmail Facebook X LinkedIn More