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Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.

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cam.issuedOnline2018-01-24
dc.contributor.authorTakahashi, Masateru
dc.contributor.authorTakahashi, Etsuko
dc.contributor.authorJoudeh, Luay I
dc.contributor.authorMarini, Monica
dc.contributor.authorDas, Gobind
dc.contributor.authorElshenawy, Mohamed M
dc.contributor.authorAkal, Anastassja
dc.contributor.authorSakashita, Kosuke
dc.contributor.authorAlam, Intikhab
dc.contributor.authorTehseen, Muhammad
dc.contributor.authorSobhy, Mohamed A
dc.contributor.authorStingl, Ulrich
dc.contributor.authorMerzaban, Jasmeen S
dc.contributor.authorDi Fabrizio, Enzo
dc.contributor.authorHamdan, Samir M
dc.contributor.orcidJoudeh, Luay [0000-0001-9338-205X]
dc.date.accessioned2018-11-05T10:25:17Z
dc.date.available2018-11-05T10:25:17Z
dc.date.issued2018-06
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 Thermococcus kodakarensis 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.format.mediumPrint-Electronic
dc.identifier.doi10.17863/CAM.31958
dc.identifier.eissn1530-6860
dc.identifier.issn0892-6638
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/284583
dc.languageeng
dc.language.isoeng
dc.publisherWiley
dc.publisher.urlhttp://dx.doi.org/10.1096/fj.201700862rr
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectDNA polymerase engineering
dc.subjecthalophilic enzymes
dc.subjectstructural adaptation
dc.subjectstructure dynamism
dc.subjectthermophilic enzymes
dc.subjectArchaeal Proteins
dc.subjectDNA-Directed DNA Polymerase
dc.subjectIndian Ocean
dc.subjectMolecular Dynamics Simulation
dc.subjectThermococcus
dc.titleDynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.
dc.typeArticle
dcterms.dateAccepted2018-01-16
prism.endingPage3360
prism.issueIdentifier6
prism.publicationDate2018
prism.publicationNameFASEB J
prism.startingPage3346
prism.volume32
rioxxterms.licenseref.startdate2018-06
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1096/fj.201700862RR

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