A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P

Yanagisawa, Tatsuo; Sumida, Tomomi; Ishii, Ryohei; Takemoto, Chie; Yokoyama, Shigeyuki
September 2010
Nature Structural & Molecular Biology;Sep2010, Vol. 17 Issue 9, p1136
Academic Journal
Aminoacyl-tRNA synthetase (aaRS) paralogs with unknown functions exist in various species. We now report novel 'protein lysylation' by an Escherichia coli lysyl-tRNA synthetase paralog, GenX/PoxA/YjeA. X-ray crystallographic analysis shows that the structure of the GenX protein resembles that of a class II aaRS. Further in vitro studies reveal that it specifically aminoacylates EF-P with lysine. The shape of the protein substrate mimics that of the L-shaped tRNA, and its lysylation site corresponds to the tRNA 3? end. Thus, we show how the aaRS architecture can be adapted to achieve aminoacylation of a specific protein. Moreover, in vivo analyses reveal that the translation elongation factor P (EF-P) lysylation by GenX is enhanced by YjeK (lysine 2,3-aminomutase paralog), which is encoded next to the EF-P gene, and might convert ?-lysyl–EF-P to ?-lysyl–EF-P. In vivo analyses indicate that the EF-P modification by GenX and YjeK is essential for cell survival.


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