title: Uncovering of a short internal peptide activates a tRNA synthetase procytokine.
abstract: In higher organisms, aminoacyl-tRNA synthetases developed receptor-mediated ex-translational functions that are activated by various natural mechanisms. Hydrogen-deuterium exchange combined with mass spectrometry and small-angle x-ray scattering showed that activation of the cytokine function of the 528-amino acid human tyrosyl-tRNA synthetase was associated with pinpointed uncovering of a miniature internal ELR tripeptide that triggers receptor signaling. The results reveal the structural simplicity of how the ex-translational function is implemented.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, La, Jolla, California 92037, USA.
authors.forename: Peter S
authors.initials: PS
authors.lastname: Lee
authors.forename: Hui-Min
authors.initials: HM
authors.lastname: Zhang
authors.forename: Alan G
authors.initials: AG
authors.lastname: Marshall
authors.forename: Xiang-Lei
authors.initials: XL
authors.lastname: Yang
authors.forename: Paul
authors.initials: P
authors.lastname: Schimmel
mesh_terms: D016207:Cytokines / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D009842:Oligopeptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018121:Receptors, Cytokine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014448:Tyrosine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D016207:Cytokines; D009842:Oligopeptides; D018121:Receptors, Cytokine; D014448:Tyrosine-tRNA Ligase