Institute of Technology, University of Tartu, Tartu, Estonia.
Nat Chem Biol. 2012 Aug;8(8):695-7. doi: 10.1038/nchembio.1001. Epub 2012 Jun 17.
Lys34 of the conserved translation elongation factor P (EF-P) is post-translationally lysinylated by YjeK and YjeA--a modification that is critical for bacterial virulence. Here we show that the currently accepted Escherichia coli EF-P modification pathway is incomplete and lacks a final hydroxylation step mediated by YfcM, an enzyme distinct from deoxyhypusine hydroxylase that catalyzes the final maturation step of eukaryotic initiation factor 5A, the eukaryotic EF-P homolog.
保守的翻译延伸因子 P(EF-P)中的赖氨酸 34 被 YjeK 和 YjeA 进行翻译后赖氨酸化修饰--这种修饰对于细菌的毒力至关重要。在这里,我们表明目前公认的大肠杆菌 EF-P 修饰途径是不完整的,缺乏由 YfcM 介导的最终羟化步骤,YfcM 是一种与脱羟鸟氨酸羟化酶不同的酶,后者催化真核起始因子 5A 的最后成熟步骤,即真核 EF-P 同源物。