Cargando…
The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts contained non-α-lysine substrates of PoxA that modified EF-P by a change in mass consistent with β–lysine, a substrate also predicted by genomic analyses. EF-P was efficient...
Autores principales: | Roy, Hervé, Zou, S. Betty, Bullwinkle, Tammy J., Wolfe, Benjamin S., Gilreath, Marla S., Forsyth, Craig J., Navarre, William W., Ibba, Michael |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3177975/ https://www.ncbi.nlm.nih.gov/pubmed/21841797 http://dx.doi.org/10.1038/nchembio.632 |
Ejemplares similares
-
An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation
por: Hausmann, Corinne D., et al.
Publicado: (2007) -
Aminoacyl-tRNA synthetases
por: Rubio Gomez, Miguel Angel, et al.
Publicado: (2020) -
Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major
por: Gowri, V S, et al.
Publicado: (2012) -
Strictly Conserved Lysine of Prolyl-tRNA Synthetase
Editing Domain Facilitates Binding and Positioning of Misacylated
tRNA(Pro)
por: Bartholow, Thomas G., et al.
Publicado: (2014) -
Mitochondrial Lysyl-tRNA Synthetase Independent Import of tRNA Lysine into Yeast Mitochondria
por: Sepuri, Naresh Babu V., et al.
Publicado: (2012)