TY  - GEN
AU  - Prezioso, Samantha M
AU  - Duong, Duc M
AU  - Kuiper, Emily G
AU  - Deng, Qiudong
AU  - Alberti, Sebastian
AU  - Conn, Graeme L
AU  - Goldberg, Joanna B
PY  - 2019
DO  - 10.1038/s41598-019-39331-x
SN  - 2045-2322
UR  - https://hdl.handle.net/20.500.12105/22776
AB  - The Pseudomonas aeruginosa methyltransferase 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...
LA  - eng
PB  - Nature Publishing Group
KW  - Body Temperature Regulation
KW  - Peptide Elongation Factor Tu
KW  - Protein Processing, Post-Translationa
KW  - Proteomics
KW  - Methyltransferases
KW  - Mutation
KW  - Protein Biosynthesis
KW  - Methylation
KW  - Pseudomonas aeruginosa
TI  - Trimethylation of Elongation Factor-Tu by the Dual Thermoregulated Methyltransferase EftM Does Not Impact Its Canonical Function in Translation
TY  - research article
ER  -