Translation of consecutive proline motifs causes ribosome stalling and requires rescue via the action of a specific translation elongation factor, EF-P in bacteria and archaeal/eukaryotic a/eIF5A. In Eukarya, Archaea, and all bacteria investigated so far, the functionality of this translation elongation factor depends on specific and rather unusual post-translational modifications. The phylum Actinobacteria, which includes the genera Corynebacterium, Mycobacterium, and Streptomyces, is of both medical and economic significance. Here, we report that EF-P is required in these bacteria in particular for the translation of proteins involved in amino acid and secondary metabolite production. Notably, EF-P of Actinobacteria species does not need any post-translational modification for activation. While the function and overall 3D structure of this EF-P type is conserved, the loop containing the conserved lysine is flanked by two essential prolines that rigidify it. Actinobacteria’s EF-P represents a unique subfamily that works without any modification.

连续脯氨酸基序的翻译会导致核糖体失速，并需要通过细菌和古细菌/真核生物a / eIF5A中特定翻译延伸因子EF-P的作用进行拯救。迄今为止，在Eukarya，古细菌和所有已调查的细菌中，这种翻译延伸因子的功能取决于特定的翻译异常修饰，而这种修饰并不常见。放线菌门，包括棒状杆菌属，分枝杆菌属和链霉菌属具有医学和经济意义。在这里，我们报道这些细菌特别是EF-P是必需的，特别是涉及氨基酸和次级代谢产物生产的蛋白质的翻译。值得注意的是，放线菌物种的EF-P不需要任何翻译后修饰即可激活。虽然保留了这种EF-P类型的功能和整体3D结构，但包含保守赖氨酸的环的两侧是使它变硬的必不可少的脯氨酸。放线菌的EF-P代表一个独特的亚家族，无需任何修饰即可起作用。