Bifunctional glutamate/proline--tRNA ligase

Definition:

Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it to the GAIT complex that binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin), suppressing their translation. Interferon-gamma can therefore redirect, in specific cells, the EPRS1 function from protein synthesis to translation inhibition. Also functions as an effector of the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake of long-chain fatty acid by adipocytes. Thereby, it also plays a role in fat metabolism and more indirectly influences lifespan.

References:

[1]. Abul Arif, et al. EPRS is a critical mTORC1-S6K1 effector that influences adiposity in mice. Nature. 2017 Feb 16;542(7641):357-361. [Content Brief]

[2]. Huihao Zhou, et al. ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. Nature. 2013 Feb 7;494(7435):121-4. [Content Brief]

[3]. C Cerini, et al. A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [Content Brief]

[4]. Prabha Sampath, et al. Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Cell. 2004 Oct 15;119(2):195-208. [Content Brief]

[5]. Abul Arif, et al. Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages. Mol Cell Biol. 2012 Dec;32(24):5046-55. [Content Brief]

[6]. Jonghyeon Son, et al. Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone. Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2136-45. [Content Brief]

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