Alcaide, MaríaStogios', Peter J.Lafraya, ÁlvaroTchigvintsev, AnatoliFlick, RobertBargiela, RafaelChernikova, Tatyana N.Reva, Oleg N.Hai, TranLeggewie, Christian C.Katzke, NadineLa Cono, ViolettaMatesanz, RuthJebbar, MohamedJaeger, Karl-ErichYakimov, Michail M.Yakunin, Alexander F.Golyshin, Peter N.Golyshina, Olga V.Savchenko, AlexeiFerrer, ManuelThe MAMBA Consortium2016-06-202016-06-202015-02Alcaide, M, Stogios, PJ, Lafraya, A, Tchigvintsev, A, Flick, R, Bargiela, R, Chernikova, TN, Reva, ON, Hai, T, Leggewie, CC, Katzke, N, La Cono, V, Matesanz, R, Jebbar, M, Jaeger, K-E, Yakimov, MM, Yakunin, AF, Golyshin, PN, Golyshina, OV, Savchenko, A, Ferrer, M & The MAMBA Consortium 2015, 'Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats', Environmental Microbiology, vol. 17, no. 2, pp. 332-345.1462-2912 (print)1462-2920 (online)10.1111/1462-2920.12660http://hdl.handle.net/2263/53239The 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 saltsaturated 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 deepsea 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.en© 2014 Society for Applied Microbiology and John Wiley & Sons Ltd.This is the pre-peer reviewed version of the following article : Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats,Environmental Microbiology, vol. 17, no. 2, pp. 332-345, 2015. doi : 10.1111/1462-2920.12660. The definite version is available at : http://onlinelibrary.wiley.comjournal/10.1111/(ISSN)1462-2920.Pressure adaptationLinkedThermal adaptationSalt-saturated marine habitatsPostprint Article