title: The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine.
abstract: The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts containing non-α-lysine substrates of PoxA modified EF-P with a change in mass consistent with addition of β-lysine, a substrate also predicted by genomic analyses. EF-P was efficiently functionally modified with (R)-β-lysine but not (S)-β-lysine or genetically encoded α-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases.
authors.affiliation: Department of Microbiology, Center for RNA Biology, Ohio State University, Columbus, Ohio, USA.
authors.forename: Hervé
authors.initials: H
authors.lastname: Roy
authors.forename: S Betty
authors.initials: SB
authors.lastname: Zou
authors.forename: Tammy J
authors.initials: TJ
authors.lastname: Bullwinkle
authors.forename: Benjamin S
authors.initials: BS
authors.lastname: Wolfe
authors.forename: Marla S
authors.initials: MS
authors.lastname: Gilreath
authors.forename: Craig J
authors.initials: CJ
authors.lastname: Forsyth
authors.forename: William W
authors.initials: WW
authors.lastname: Navarre
authors.forename: Michael
authors.initials: M
authors.lastname: Ibba
mesh_terms: D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D008250:Lysine-tRNA Ligase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism
chemical_list: D010445:Peptide Elongation Factors; C020746:factor EF-P; C065591:beta-lysine; D008250:Lysine-tRNA Ligase; D008239:Lysine