NDLI: (R)-β-Lysine-modified Elongation Factor P Functions in Translation Elongation

Content Provider	Journal of Biological Chemistry (JBC)
Author	Bullwinkle, Tammy J. Zou, S. Betty Rajkovic, Andrei Hersch, Steven J. Elgamal, Sara Robinson, Nathaniel Smil, David Bolshan, Yuri Navarre, William Wiley Ibba, Michael
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.
Related Links	http://www.jbc.org/content/288/6/4416.abstract
Ending Page	4423
Starting Page	4416
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	6
Volume Number	288
DOI	10.1074/jbc.M112.438879
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2013-02-08
Access Restriction	Open
Subject Keyword	Pathogenesis Post-translational Modification Protein Synthesis Ribosomes Translation Elongation Factors Microbiology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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