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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-09-06

AUTHORS

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

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. More... »

PAGES

32816

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep32816

DOI

http://dx.doi.org/10.1038/srep32816

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025949865

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27595789


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