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

Handle URI:
http://hdl.handle.net/10754/622020
Title:
High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes
Authors:
Martinez, N.; Michoud, Gregoire ( 0000-0003-1071-9900 ) ; Cario, A.; Ollivier, J.; Franzetti, B.; Jebbar, M.; Oger, P.; Peters, J.
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Martinez N, Michoud G, Cario A, Ollivier J, Franzetti B, et al. (2016) High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes. Scientific Reports 6: 32816. Available: http://dx.doi.org/10.1038/srep32816.
Publisher:
Springer Nature
Journal:
Scientific Reports
Issue Date:
6-Sep-2016
DOI:
10.1038/srep32816
Type:
Article
ISSN:
2045-2322
Sponsors:
We are gratefully acknowledging the help of B. Frick for the measurement on IN16 and of M.M. Koza for the measurement on IN6, the ILL for allocation of beam time and the financing of the Agence Nationale de la Recherche (ANR; project number ANR 2010 BLAN 1725 01 Living deep).
Additional Links:
http://www.nature.com/articles/srep32816
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorMartinez, N.en
dc.contributor.authorMichoud, Gregoireen
dc.contributor.authorCario, A.en
dc.contributor.authorOllivier, J.en
dc.contributor.authorFranzetti, B.en
dc.contributor.authorJebbar, M.en
dc.contributor.authorOger, P.en
dc.contributor.authorPeters, J.en
dc.date.accessioned2016-12-14T08:30:13Z-
dc.date.available2016-12-14T08:30:13Z-
dc.date.issued2016-09-06en
dc.identifier.citationMartinez N, Michoud G, Cario A, Ollivier J, Franzetti B, et al. (2016) High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes. Scientific Reports 6: 32816. Available: http://dx.doi.org/10.1038/srep32816.en
dc.identifier.issn2045-2322en
dc.identifier.doi10.1038/srep32816en
dc.identifier.urihttp://hdl.handle.net/10754/622020-
dc.description.abstractWater 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.en
dc.description.sponsorshipWe are gratefully acknowledging the help of B. Frick for the measurement on IN16 and of M.M. Koza for the measurement on IN6, the ILL for allocation of beam time and the financing of the Agence Nationale de la Recherche (ANR; project number ANR 2010 BLAN 1725 01 Living deep).en
dc.publisherSpringer Natureen
dc.relation.urlhttp://www.nature.com/articles/srep32816en
dc.rightsThis work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleHigh protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalScientific Reportsen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionInstitut Laue Langevin, Grenoble Cedex 9, Franceen
dc.contributor.institutionUniv. Grenoble Alpes, IBS, Grenoble Cedex 9, Franceen
dc.contributor.institutionUniv. Brest, CNRS, Ifremer, LM2E, IUEM, Plouzané, Franceen
dc.contributor.institutionUniv Lyon, ENS Lyon, CNRS UMR 5276, Lyon Cedex 07, Franceen
dc.contributor.institutionUniv Lyon, INSA Lyon, CNRS UMR 5240, Villeurbanne Cedex, Franceen
dc.contributor.institutionUniv. Grenoble Alpes, LiPhy, Grenoble Cedex 9, Franceen
kaust.authorMichoud, Gregoireen
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