Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes
AuthorsGrötzinger, Stefan W.
Al Rowaihi, Israa
Archer, John A.C.
Arold, Stefan T.
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Computational Bioscience Research Center (CBRC)
KAUST Catalysis Center (KCC)
Physical Sciences and Engineering (PSE) Division
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AbstractBecause only 0.01% of prokaryotic genospecies can be cultured and in situ observations are often impracticable, culture-independent methods are required to understand microbial life and harness potential applications of microbes. Here, we report a methodology for the production of proteins with desired functions based on single amplified genomes (SAGs) from unculturable species. We use this method to resurrect an alcohol dehydrogenase (ADH/D1) from an uncharacterized halo-thermophilic archaeon collected from a brine pool at the bottom of the Red Sea. Our crystal structure of 5,6-dihydroxy NADPH-bound ADH/D1 combined with biochemical analyses reveal the molecular features of its halo-thermophily, its unique habitat adaptations, and its possible reaction mechanism for atypical oxygen activation. Our strategy offers a general guide for using SAGs as a source for scientific and industrial investigations of ‘microbial dark matter’.
CitationGrötzinger SW, Karan R, Strillinger E, Bader S, Frank A, et al. (2017) Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes. ACS Chemical Biology. Available: http://dx.doi.org/10.1021/acschembio.7b00792.
SponsorsThe research reported in this publication was supported by the King Abdullah University of Science and Technology (KAUST) through the baseline fund and the Office of Sponsored Research (OSR) under award nos. URF/1/1976.06, URF/1/2602.01.01, and URF/1/1974. The authors are thankful for support for E.S. and S.G. from the International Graduate School of Science and Engineering (IGGSE), Technical University of Munich (TUM), project 8.03.
PublisherAmerican Chemical Society (ACS)
JournalACS Chemical Biology