(R)-β-lysine Modified Elongation Factor P Functions in Translation Elongation

Authors

Tammy J. Bullwinkle, The Ohio State University
S. Betty Zou, University of Toronto
Andrei Rajkovic, The Ohio State University
Steven J. Hersch, University of Toronto
Sara Elgamal, The Ohio State University
Nathaniel Robinson, The Ohio State University
David Smil, University of Toronto
Yuri Bolshan, University of Toronto
William Wiley Navarre, University of Toronto
Michael Ibba, Chapman UniversityFollow

Document Type

Article

Publication Date

12-31-2012

Abstract

Post-translational modification of bacterial elongation factor P (EF-P) with (R)-β-lysine at a conserved lysine residue activates the protein in vivo and increases puromycin reactivity of the ribosome in vitro. The additional hydroxylation of EF-P at the same lysine residue by the YfcM protein has also recently been described. The roles of modified and unmodified EF-P during different steps in translation, and how this correlates to its physiological role in the cell, have recently been linked to the synthesis of polyproline stretches in proteins. Polysome analysis indicated that EF-P functions in translation elongation, rather than initiation as proposed previously. This was further supported by the inability of EF-P to enhance the rate of formation of fMet-Lys or fMet-Phe, indicating that the role of EF-P is not to specifically stimulate formation of the first peptide bond. Investigation of hydroxyl-(β)-lysyl-EF-P showed 30% increased puromycin reactivity but no differences in dipeptide synthesis rates when compared with the β-lysylated form. Unlike disruption of the other genes required for EF-P modification, deletion of yfcM had no phenotypic consequences in Salmonella. Taken together, our findings indicate that EF-P functions in translation elongation, a role critically dependent on post-translational β-lysylation but not hydroxylation.

Comments

This article was originally published in Journal of Biological Chemistry, volume 288, in 2013. https://doi.org/10.1074/jbc.M112.438879

Recommended Citation

Bullwinkle, T.J., Zou, S.B., Rajkovic, A., Hersch, S.J., Elgamal, S., Robinson, N., Smil, D., Bolshan, Y., Navarre, W.W. and Ibba, M. (2013) (R)-β-lysine modified elongation factor P functions in translation elongation. J. Biol. Chem 288, 4416-4423. https://doi.org/10.1074/jbc.M112.438879

Copyright

American Society for Biochemistry and Molecular Biology