| Literature DB >> 26376634 |
Pierre Vauclare1,2,3, Vincent Marty1,2,3, Elisa Fabiani1,2,3,4, Nicolas Martinez1,2,3,4, Marion Jasnin4, Frank Gabel1,2,3, Judith Peters1,4, Giuseppe Zaccai1,4, Bruno Franzetti5,6,7,8.
Abstract
Halobacterium salinarum is an extreme halophile archaeon with an absolute requirement for a multimolar salt environment. It accumulates molar concentrations of KCl in the cytosol to counterbalance the external osmotic pressure imposed by the molar NaCl. As a consequence, cytosolic proteins are permanently exposed to low water activity and highly ionic conditions. In non-adapted systems, such conditions would promote protein aggregation, precipitation, and denaturation. In contrast, in vitro studies showed that proteins from extreme halophilic cells are themselves obligate halophiles. In this paper, adaptation via dynamics to low-salt stress in H. salinarum cells was measured by neutron scattering experiments coupled with microbiological characterization. The molecular dynamic properties of a proteome represent a good indicator for environmental adaptation and the neutron/microbiology approach has been shown to be well tailored to characterize these modifications. In their natural setting, halophilic organisms often have to face important variations in environmental salt concentration. The results showed deleterious effects already occur in the H. salinarum proteome, even when the external salt concentration is still relatively high, suggesting the onset of survival mechanisms quite early when the environmental salt concentration decreases.Entities:
Keywords: Enzyme structure; Function; Function of extremophiles; Halophiles; Macromolecular structure; Protein stability
Mesh:
Substances:
Year: 2015 PMID: 26376634 DOI: 10.1007/s00792-015-0782-x
Source DB: PubMed Journal: Extremophiles ISSN: 1431-0651 Impact factor: 2.395