The C-terminal helix of Pseudomonas aeruginosa elongation factor Ts tunes EFT-Tu dynamics to modulate nucleotide exchange

dc.contributor.authorDe Laurentiis, Evelina I.
dc.contributor.authorMercier, Evan
dc.contributor.authorWieden, Hans-Joachim
dc.date.accessioned2019-12-18T22:41:28Z
dc.date.available2019-12-18T22:41:28Z
dc.date.issued2015
dc.descriptionSherpa Romeo green journal. Permission to archive final published versionen_US
dc.description.abstractLittle is known about the conservation of critical kinetic parameters and the mechanistic strategies of elongation factor (EF) Ts-catalyzed nucleotide exchange in EF-Tu in bacteria and particularly in clinically relevant pathogens. EF-Tu from the clinically relevant pathogen Pseudomonas aeruginosa shares over 84% sequence identity with the corresponding elongation factor from Escherichia coli. Interestingly, the functionally closely linked EF-Ts only shares 55% sequence identity. To identify any differences in the nucleotide binding properties, as well as in the EF-Ts-mediated nucleotide exchange reaction, we performed a comparative rapid kinetics and mutagenesis analysis of the nucleotide exchange mechanism for both the E. coli and P. aeruginosa systems, identifying helix 13 of EF-Ts as a previously unnoticed regulatory element in the nucleotide exchange mechanism with species-specific elements. Our findings support the base side-first entry of the nucleotide into the binding pocket of the EF-Tu·EF-Ts binary complex, followed by displacement of helix 13 and rapid binding of the phosphate side of the nucleotide, ultimately leading to the release of EF-Ts.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationDe Laurentiis, E. I., Mercier, E., & Wieden, H.-J. (2016). The C-terminal helix of Pseudomonas aeruginosa elongation factor Ts tunes EF-Tu dynamics to modulate nucleotide exchange. Journal of Biological Chemistry, 291(44), 23136-023148. doi:10.1074/jbc.M116.740381en_US
dc.identifier.urihttps://hdl.handle.net/10133/5639
dc.language.isoen_USen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://dx.doi.org/10.1074/jbc.M116.740381
dc.subjectGTPaseen_US
dc.subjectMolecular dynamicsen_US
dc.subjectPre-steady-state kineticsen_US
dc.subjectPseudomonas aeruginosa (P. aeruginosa)en_US
dc.subjectTranslation elongation factoren_US
dc.subjectElongation factor Tsen_US
dc.subjectElongation factor Tuen_US
dc.subjectCatalytic mechanismen_US
dc.subjectNucleotide bindingen_US
dc.subjectNucleotide exchangeen_US
dc.titleThe C-terminal helix of Pseudomonas aeruginosa elongation factor Ts tunes EFT-Tu dynamics to modulate nucleotide exchangeen_US
dc.typeArticleen_US
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