大肠杆菌
翻译(生物学)
生物化学
亚科
突变体
EF图
氨基酸
化学
核糖体
延伸系数
蛋白质生物合成
赖氨酸
细胞生物学
生物
核糖核酸
信使核糖核酸
基因
作者
Urte Tomasiunaite,Pavel Kielkowski,Ralph Krafczyk,Ignasi Forné,Axel Imhof,Kirsten Jung
出处
期刊:Cell Reports
[Elsevier]
日期:2024-05-01
卷期号:43 (5): 114063-114063
标识
DOI:10.1016/j.celrep.2024.114063
摘要
Summary
Bacteria overcome ribosome stalling by employing translation elongation factor P (EF-P), which requires post-translational modification (PTM) for its full activity. However, EF-Ps of the PGKGP subfamily are unmodified. The mechanism behind the ability to avoid PTM while retaining active EF-P requires further examination. Here, we investigate the design principles governing the functionality of unmodified EF-Ps in Escherichia coli. We screen for naturally unmodified EF-Ps with activity in E. coli and discover that the EF-P from Rhodomicrobium vannielii rescues growth defects of a mutant lacking the modification enzyme EF-P-(R)-β-lysine ligase. We identify amino acids in unmodified EF-P that modulate its activity. Ultimately, we find that substitution of these amino acids in other marginally active EF-Ps of the PGKGP subfamily leads to fully functional variants in E. coli. These results provide strategies to improve heterologous expression of proteins with polyproline motifs in E. coli and give insights into cellular adaptations to optimize protein synthesis.
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