Trimethylation of Elongation Factor-Tu by the Dual Thermoregulated Methyltransferase EftM Does Not Impact Its Canonical Function in Translation.
Trimethylation of Elongation Factor-Tu by the Dual Thermoregulated Methyltransferase EftM Does Not Impact Its Canonical Function in Translation.
复制标题
双温控甲基转移酶 EftM 对伸长因子-Tu 的三甲基化不会影响其翻译中的典型功能。
DOI：
10.1038/s41598-019-39331-x
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发表时间：
2019
影响因子：
4.6
通讯作者：
Goldberg,JoannaB
中科院分区：
文献类型：
--
作者：
Prezioso,SamanthaM;Duong,DucM;Kuiper,EmilyG;Deng,Qiudong;Albertí,Sebastián;Conn,GraemeL;Goldberg,JoannaB
ThePseudomonas aeruginosamethyltransferase EftM trimethylates elongation factor-Tu (EF-Tu) on lysine 5 to form a post-translational modification important for initial bacterial adherence to host epithelial cells. EftM methyltransferase activity is directly temperature regulated. The protein stability of EftM is tuned with a melting temperature (Tm) around 37 °C such that the enzyme is stable and active at 25 °C, but is completely inactivated by protein unfolding at higher temperatures. This leads to higher observable levels of EF-Tu trimethylation at the lower temperature. Here we report an additional layer of thermoregulation resulting in lowereftMmRNA transcript level at 37 °C compared to 25 °C and show that this regulation occurs at the level of transcription initiation. To begin to define the impact of this system onP.aeruginosaphysiology, we demonstrate that EF-Tu is the only observable substrate for EftM. Further, we interrogated the proteome of three different wild-typeP.aeruginosastrains, theireftMmutants, and these mutants complemented witheftMand conclude that trimethylation of EF-Tu by EftM does not impact EF-Tu’s canonical function in translation. In addition to furthering our knowledge of thisPseudomonasvirulence factor, this study provides an intriguing example of a protein with multiple layers of thermoregulation.
