Uncovering of a Short Internal Peptide Activates a tRNA Synthetase Procytokine
Uncovering of a Short Internal Peptide Activates a tRNA Synthetase Procytokine
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DOI：
10.1074/jbc.c112.369439
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发表时间：
2012-06-08
影响因子：
4.8
通讯作者：
Schimmel, Paul
中科院分区：
文献类型：
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作者：
Lee, Peter S.;Zhang, Hui-Min;Schimmel, Paul
在高等生物中，氨酰基-tRNA 合成酶发展出受体介导的翻译外功能，该功能由各种自然机制激活。氢-氘交换结合质谱和小角 X 射线散射表明，528 个氨基酸的人酪氨酰-tRNA 合成酶的细胞因子功能的激活与触发受体信号传导的微型内部 ELR 三肽的精确揭示相关。结果揭示了如何实现外翻译函数的结构简单性。
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.