Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex

Benjamin J. Burnett; Roger B. Altman; Ryan Ferrao; Jose L. Alejo; Navdep Kaur; Joshua Kanji; Scott C. Blanchard

doi:10.1074/jbc.M113.460014

Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex

Benjamin J. Burnett, Roger B. Altman, Ryan Ferrao, Jose L. Alejo, Navdep Kaur, Joshua Kanji, Scott C. Blanchard

Genetics, Cell Biology and Development (CBS)

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

Abstract

Background: Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP. Results: EF-Tu·GTP·aa-tRNA ternary complex formation and decay rates are accelerated in the presence of the nucleotide exchange factor elongation factor Ts (EF-Ts). Conclusion: EF-Ts directly facilitates the formation and disassociation of ternary complex. Significance: This system demonstrates a novel function of EF-Ts.

Original language	English (US)
Pages (from-to)	13917-13928
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	288
Issue number	19
DOIs	https://doi.org/10.1074/jbc.M113.460014
State	Published - May 10 2013

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title = "Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex",

abstract = "Background: Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP. Results: EF-Tu·GTP·aa-tRNA ternary complex formation and decay rates are accelerated in the presence of the nucleotide exchange factor elongation factor Ts (EF-Ts). Conclusion: EF-Ts directly facilitates the formation and disassociation of ternary complex. Significance: This system demonstrates a novel function of EF-Ts.",

author = "Burnett, {Benjamin J.} and Altman, {Roger B.} and Ryan Ferrao and Alejo, {Jose L.} and Navdep Kaur and Joshua Kanji and Blanchard, {Scott C.}",

year = "2013",

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doi = "10.1074/jbc.M113.460014",

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T1 - Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex

AU - Burnett, Benjamin J.

AU - Altman, Roger B.

AU - Ferrao, Ryan

AU - Alejo, Jose L.

AU - Kaur, Navdep

AU - Kanji, Joshua

AU - Blanchard, Scott C.

PY - 2013/5/10

Y1 - 2013/5/10

N2 - Background: Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP. Results: EF-Tu·GTP·aa-tRNA ternary complex formation and decay rates are accelerated in the presence of the nucleotide exchange factor elongation factor Ts (EF-Ts). Conclusion: EF-Ts directly facilitates the formation and disassociation of ternary complex. Significance: This system demonstrates a novel function of EF-Ts.

AB - Background: Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP. Results: EF-Tu·GTP·aa-tRNA ternary complex formation and decay rates are accelerated in the presence of the nucleotide exchange factor elongation factor Ts (EF-Ts). Conclusion: EF-Ts directly facilitates the formation and disassociation of ternary complex. Significance: This system demonstrates a novel function of EF-Ts.

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DO - 10.1074/jbc.M113.460014

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SN - 0021-9258

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EP - 13928

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 19

ER -

Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex

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