Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.
Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.
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DOI：
10.1016/j.celrep.2020.03.009
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发表时间：
2020-03
期刊：
影响因子：
8.8
通讯作者：
Bruno Pinheiro;C. Scheidler;P. Kielkowski;M. Schmid;I. Forné;Suhui Ye;N. Reiling;E. Takano;A. Imhof;S. Sieber;S. Schneider;K. Jung
中科院分区：
文献类型：
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作者：
Bruno Pinheiro;C. Scheidler;P. Kielkowski;M. Schmid;I. Forné;Suhui Ye;N. Reiling;E. Takano;A. Imhof;S. Sieber;S. Schneider;K. Jung
连续脯氨酸基序的翻译导致核糖体停滞，并且需要通过细菌和古细菌/真核生物a/eIF 5A中的特异性翻译延伸因子EF-P的作用进行拯救。在真核生物，古细菌，和所有的细菌研究到目前为止，这种翻译延伸因子的功能取决于特定的和相当不寻常的翻译后修饰。放线菌门包括棒状杆菌属、分枝杆菌属和链霉菌属，具有医学和经济双重意义。在这里，我们报告说，EF-P是需要在这些细菌中，特别是参与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来激活。虽然这种EF-P类型的功能和整体3D结构是保守的，但含有保守赖氨酸的环两侧是两个必需的脯氨酸，使其刚性化。放线菌的EF-P代表了一个独特的亚家族，无需任何修饰即可工作。
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 generaCorynebacterium,Mycobacterium, andStreptomyces, 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.