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dc.contributor.authorTakahashi, Masateru
dc.contributor.authorTakahashi, Etsuko
dc.contributor.authorJoudeh, Luay
dc.contributor.authorMarini, Monica
dc.contributor.authorDas, Gobind
dc.contributor.authorElshenawy, Mohamed
dc.contributor.authorGespers (Akal), Anastassja
dc.contributor.authorSakashita, Kosuke
dc.contributor.authorAlam, Intikhab
dc.contributor.authorTehseen, Muhammad
dc.contributor.authorSobhy, Mohamed Abdelmaboud
dc.contributor.authorStingl, Ulrich
dc.contributor.authorMerzaban, Jasmeen
dc.contributor.authorDi Fabrizio, Enzo M.
dc.contributor.authorHamdan, Samir
dc.date.accessioned2018-01-30T08:08:08Z
dc.date.available2018-01-30T08:08:08Z
dc.date.issued2018-01-24
dc.identifier.citationTakahashi 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.
dc.identifier.issn0892-6638
dc.identifier.issn1530-6860
dc.identifier.pmid29401622
dc.identifier.doi10.1096/fj.201700862rr
dc.identifier.urihttp://hdl.handle.net/10754/626952
dc.description.abstractThe 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.
dc.description.sponsorshipThe 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.
dc.publisherFASEB
dc.relation.urlhttp://www.fasebj.org/doi/10.1096/fj.201700862RR
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
dc.subjectDNA polymerase engineering
dc.subjecthalophilic enzymes
dc.subjectthermophilic enzymes
dc.subjectstructure dynamism
dc.subjectstructural adaptation
dc.titleDynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentChemical Engineering Program
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
dc.contributor.departmentKAUST Catalysis Center (KCC)
dc.contributor.departmentLaboratory of DNA Replication and Recombination
dc.contributor.departmentMarine Microbial Ecology Research Group
dc.contributor.departmentMarine Science Program
dc.contributor.departmentMaterial Science and Engineering Program
dc.contributor.departmentOffice of the VP
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.contributor.departmentProteomics and Protein Expression
dc.contributor.departmentRed Sea Research Center (RSRC)
dc.identifier.journalThe FASEB Journal
dc.eprint.versionPost-print
dc.contributor.institutionFort Lauderdale Research and Education Center, University of Florida, Davie, Florida, USA
kaust.personTakahashi, Masateru
kaust.personTakahashi, Etsuko
kaust.personJoudeh, Luay
kaust.personMarini, Monica
kaust.personDas, Gobind
kaust.personElshenawy, Mohamed
kaust.personAkal, Anastassja
kaust.personSakashita, Kosuke
kaust.personAlam, Intikhab
kaust.personTehseen, Muhammad
kaust.personSobhy, Mohamed Abdelmaboud
kaust.personStingl, Ulrich
kaust.personMerzaban, Jasmeen S.
kaust.personDi Fabrizio, Enzo M.
kaust.personHamdan, Samir
refterms.dateFOA2019-11-13T13:17:20Z
dc.date.published-online2018-01-24
dc.date.published-print2018-06


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