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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.

SUBMITTER: Lee PS

PROVIDER: S-EPMC3370235 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature

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Uncovering of a short internal peptide activates a tRNA synthetase procytokine.

Lee Peter S PS Zhang Hui-Min HM Marshall Alan G AG Yang Xiang-Lei XL Schimmel Paul P

The Journal of biological chemistry 20120501 24

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 simpl ...[more]

PMID: 22549774

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