Hong Hye-Rim, Prince Cassidy R, Tetreault Daniel D, Wu Letian, Feaga Heather A
Department of Microbiology, Cornell University, Ithaca, NY 14853.
bioRxiv. 2023 Dec 5:2023.08.04.552005. doi: 10.1101/2023.08.04.552005.
Protein synthesis is performed by the ribosome and a host of highly conserved elongation factors. Elongation factor P (EF-P) prevents ribosome stalling at difficult-to-translate sequences, particularly polyproline tracts. In bacteria, phenotypes associated with deletion range from modest to lethal, suggesting that some species encode an additional translation factor that has similar function to EF-P. Here we identify YfmR as a translation factor that is essential in the absence of EF-P in . YfmR is an ABCF ATPase that is closely related to both Uup and EttA, ABCFs that bind the ribosomal E-site and are conserved in more than 50% of bacterial genomes. We show that YfmR associates with actively translating ribosomes and that depleting YfmR from Δ cells causes severe ribosome stalling at a polyproline tract . YfmR depletion from Δ cells was lethal, and caused reduced levels of actively translating ribosomes. Our results therefore identify YfmR as an important translation factor that is essential in in the absence of EF-P.
蛋白质合成由核糖体和许多高度保守的延伸因子完成。延伸因子P（EF-P）可防止核糖体在难以翻译的序列处停滞，尤其是多聚脯氨酸序列。在细菌中，与缺失相关的表型从轻微到致命不等，这表明一些物种编码了一种与EF-P功能相似的额外翻译因子。在这里，我们确定YfmR是一种在缺乏EF-P时对[具体物种]至关重要的翻译因子。YfmR是一种ABCF型ATP酶，与Uup和EttA密切相关，这两种ABCF蛋白结合核糖体E位点，在超过50%的细菌基因组中保守存在。我们发现YfmR与正在进行翻译的核糖体相关联，并且从[具体缺失EF-P的细胞系]细胞中耗尽YfmR会导致在多聚脯氨酸序列处严重的核糖体停滞。从[具体缺失EF-P的细胞系]细胞中耗尽YfmR是致命的，并导致正在进行翻译的核糖体水平降低。因此，我们的结果确定YfmR是一种在缺乏EF-P时对[具体物种]至关重要的重要翻译因子。
