Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats

Alcaide, M. and Stogios, P.J. and Lafraya, A. and Tchigvintsev, A. and Flick, R. and Bargiela, R. and Chernikova, T.N. and Reva, O.N. and Hai, T. and Leggewie, C.C. and Katzke, N. and La Cono, V. and Matesanz, R. and Jebbar, M and Jaeger, K. and Yakimov, M.M. and Yakunin, A.F. and Golyshin, P.N. and Golyshina, O.V. and Savchenko, A. and Ferrer, M. and The MAMBA Consortium., (2014) Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats. Environmental Microbiology, 17 (2). pp. 332-345. DOI: 10.1111/1462-2920.12660

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The present study provides a deeper view of protein functionality as a function of temperature, salt and pressure in deep-sea habitats. A set of eight different enzymes from five distinct deep-sea (3040�4908�m depth), moderately warm (14.0�16.5°C) biotopes, characterized by a wide range of salinities (39�348 practical salinity units), were investigated for this purpose. An enzyme from a �superficial� marine hydrothermal habitat (65°C) was isolated and characterized for comparative purposes. We report here the first experimental evidence suggesting that in salt-saturated deep-sea habitats, the adaptation to high pressure is linked to high thermal resistance (P value�=�0.0036). Salinity might therefore increase the temperature window for enzyme activity, and possibly microbial growth, in deep-sea habitats. As an example, Lake Medee, the largest hypersaline deep-sea anoxic lake of the Eastern Mediterranean Sea, where the water temperature is never higher than 16°C, was shown to contain halopiezophilic-like enzymes that are most active at 70°C and with denaturing temperatures of 71.4°C. The determination of the crystal structures of five proteins revealed unknown molecular mechanisms involved in protein adaptation to poly-extremes as well as distinct active site architectures and substrate preferences relative to other structurally characterized enzymes.

Item Type: Article
Subjects: Research Publications
Departments: College of Natural Sciences > School of Biological Sciences
Date Deposited: 02 Apr 2016 03:14
Last Modified: 02 Apr 2016 03:14
ISSN: 1462-2920
URI: http://e.bangor.ac.uk/id/eprint/6439
Identification Number: DOI: 10.1111/1462-2920.12660
Publisher: Wiley
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