High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes

N. Martinez, Gregoire Michoud, A. Cario, J. Ollivier, B. Franzetti, M. Jebbar, P. Oger, J. Peters

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Water and protein dynamics on a nanometer scale were measured by quasi-elastic neutron scattering in the piezophile archaeon Thermococcus barophilus and the closely related pressure-sensitive Thermococcus kodakarensis, at 0.1 and 40 MPa. We show that cells of the pressure sensitive organism exhibit higher intrinsic stability. Both the hydration water dynamics and the fast protein and lipid dynamics are reduced under pressure. In contrast, the proteome of T. barophilus is more pressure sensitive than that of T. kodakarensis. The diffusion coefficient of hydration water is reduced, while the fast protein and lipid dynamics are slightly enhanced with increasing pressure. These findings show that the coupling between hydration water and cellular constituents might not be simply a master-slave relationship. We propose that the high flexibility of the T. barophilus proteome associated with reduced hydration water may be the keys to the molecular adaptation of the cells to high hydrostatic pressure.
Original languageEnglish (US)
JournalScientific Reports
Volume6
Issue number1
DOIs
StatePublished - Sep 6 2016

Fingerprint Dive into the research topics of 'High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes'. Together they form a unique fingerprint.

Cite this