Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea
Type
ArticleAuthors
Takahashi, MasateruTakahashi, Etsuko
Joudeh, Luay

Marini, Monica

Das, Gobind

Elshenawy, Mohamed

Gespers (Akal), Anastassja

Sakashita, Kosuke

Alam, Intikhab
Tehseen, Muhammad

Sobhy, Mohamed Abdelmaboud
Stingl, Ulrich

Merzaban, Jasmeen

Di Fabrizio, Enzo M.

Hamdan, Samir

KAUST Department
Biological and Environmental Sciences and Engineering (BESE) DivisionBioscience Program
Chemical Engineering Program
Computational Bioscience Research Center (CBRC)
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
KAUST Catalysis Center (KCC)
Laboratory of DNA Replication and Recombination
Marine Microbial Ecology Research Group
Marine Science Program
Material Science and Engineering Program
Office of the VP
Physical Science and Engineering (PSE) Division
Proteomics and Protein Expression
Red Sea Research Center (RSRC)
Date
2018-01-24Online Publication Date
2018-01-24Print Publication Date
2018-06Permanent link to this record
http://hdl.handle.net/10754/626952
Metadata
Show full item recordAbstract
The deep-sea brines of the Red Sea are remote and unexplored environments characterized by high temperatures, anoxic water, and elevated concentrations of salt and heavy metals. This environment provides a rare system to study the interplay between halophilic and thermophilic adaptation in biologic macromolecules. The present article reports the first DNA polymerase with halophilic and thermophilic features. Biochemical and structural analysis by Raman and circular dichroism spectroscopy showed that the charge distribution on the protein’s surface mediates the structural balance between stability for thermal adaptation and flexibility for counteracting the salt-induced rigid and nonfunctional hydrophobic packing. Salt bridge interactions via increased negative and positive charges contribute to structural stability. Salt tolerance, conversely, is mediated by a dynamic structure that becomes more fixed and functional with increasing salt concentration. We propose that repulsive forces among excess negative charges, in addition to a high percentage of negatively charged random coils, mediate this structural dynamism. This knowledge enabled us to engineer a halophilic version of KOD DNA polymerase.—Takahashi, M., Takahashi, E., Joudeh, L. I., Marini, M., Das, G., Elshenawy, M. M., Akal, A., Sakashita, K., Alam, I., Tehseen, M., Sobhy, M. A., Stingl, U., Merzaban, J. S., Di Fabrizio, E., Hamdan, S. M. Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.Citation
Takahashi M, Takahashi E, Joudeh LI, Marini M, Das G, et al. (2018) Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea. The FASEB Journal: fj.201700862RR. Available: http://dx.doi.org/10.1096/fj.201700862rr.Sponsors
The authors thank the King Abdullah University of Science and Technology (KAUST) BioScience Core Laboratory for providing Pfu polymerase. This research was funded by the Saudi Economic and Development Company (SEDCO) Research Excellence Project and baseline funding from KAUST to S.M.H. The authors declare no conflicts of interest.Publisher
FASEBJournal
The FASEB JournalPubMed ID
29401622Additional Links
http://www.fasebj.org/doi/10.1096/fj.201700862RRae974a485f413a2113503eed53cd6c53
10.1096/fj.201700862rr
Scopus Count
Collections
Articles; Biological and Environmental Sciences and Engineering (BESE) Division; Red Sea Research Center (RSRC); Bioscience Program; Marine Science Program; Physical Science and Engineering (PSE) Division; Chemical Engineering Program; Material Science and Engineering Program; KAUST Catalysis Center (KCC); Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) DivisionRelated articles
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