期刊
ENVIRONMENTAL MICROBIOLOGY
卷 17, 期 2, 页码 332-345出版社
WILEY
DOI: 10.1111/1462-2920.12660
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资金
- European Community project MAMBA [FP7-KBBE-2008-226977]
- Spanish Ministry of Economy and Competitiveness [BIO2011-25012]
- European Commission [FP7-OCEAN.2011-2, 287589]
- Government of Canada through Genome Canada
- Ontario Genomics Institute [2009-OGI-ABC-1405]
- U.S. National Institutes of Health (through the Midwest Center for Structural Genomics) [GM074942, GM094585]
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 (3040-4908m depth), moderately warm (14.0-16.5 degrees 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 degrees 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 degrees C, was shown to contain halopiezophilic-like enzymes that are most active at 70 degrees C and with denaturing temperatures of 71.4 degrees 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.
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