The C-terminal helix of Pseudomonas aeruginosa elongation factor Ts tunes EFT-Tu dynamics to modulate nucleotide exchange
dc.contributor.author | De Laurentiis, Evelina I. | |
dc.contributor.author | Mercier, Evan | |
dc.contributor.author | Wieden, Hans-Joachim | |
dc.date.accessioned | 2019-12-18T22:41:28Z | |
dc.date.available | 2019-12-18T22:41:28Z | |
dc.date.issued | 2015 | |
dc.description | Sherpa Romeo green journal. Permission to archive final published version | en_US |
dc.description.abstract | Little 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-TuĀ·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-review | Yes | en_US |
dc.identifier.citation | De 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.M116.740381 | en_US |
dc.identifier.uri | https://hdl.handle.net/10133/5639 | |
dc.language.iso | en_US | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology | en_US |
dc.publisher.department | Department of Chemistry and Biochemistry | en_US |
dc.publisher.faculty | Arts and Science | en_US |
dc.publisher.institution | University of Lethbridge | en_US |
dc.publisher.url | https://dx.doi.org/10.1074/jbc.M116.740381 | |
dc.subject | GTPase | en_US |
dc.subject | Molecular dynamics | en_US |
dc.subject | Pre-steady-state kinetics | en_US |
dc.subject | Pseudomonas aeruginosa (P. aeruginosa) | en_US |
dc.subject | Translation elongation factor | en_US |
dc.subject | Elongation factor Ts | en_US |
dc.subject | Elongation factor Tu | en_US |
dc.subject | Catalytic mechanism | en_US |
dc.subject | Nucleotide binding | en_US |
dc.subject | Nucleotide exchange | en_US |
dc.title | The C-terminal helix of Pseudomonas aeruginosa elongation factor Ts tunes EFT-Tu dynamics to modulate nucleotide exchange | en_US |
dc.type | Article | en_US |