Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes
Type
ArticleAuthors
Grötzinger, Stefan W.Karan, Ram
Strillinger, Eva

Bader, Stefan
Frank, Annika
Al Rowaihi, Israa

Gespers (Akal), Anastassja

Wackerow, Wiebke
Archer, John A.C.

Rueping, Magnus

Weuster-Botz, Dirk
Groll, Michael
Eppinger, Jörg

Arold, Stefan T.

KAUST Department
Biological & Organometallic Catalysis LaboratoriesBiological and Environmental Sciences and Engineering (BESE) Division
Bioscience Program
Chemical Science Program
Computational Bioscience Research Center (CBRC)
KAUST Catalysis Center (KCC)
Office of the VP
Physical Science and Engineering (PSE) Division
Structural Biology and Engineering
KAUST Grant Number
URF/1/1976.06URF/1/2602.01.01
URF/1/1974
Date
2017-12-18Online Publication Date
2017-12-18Print Publication Date
2018-01-19Permanent link to this record
http://hdl.handle.net/10754/626319
Metadata
Show full item recordAbstract
Because 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’.Citation
Grötzinger 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.Sponsors
The 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.Publisher
American Chemical Society (ACS)Journal
ACS Chemical BiologyAdditional Links
http://pubs.acs.org/doi/abs/10.1021/acschembio.7b00792ae974a485f413a2113503eed53cd6c53
10.1021/acschembio.7b00792