5xln
From Proteopedia
Crystal structure of the TRS_UNE-T and 4EHP complex
Structural highlights
Function[IF4E2_HUMAN] Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation (PubMed:9582349, PubMed:17368478, PubMed:25624349). Acts as a repressor of translation initiation (PubMed:22751931). In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap (By similarity).[UniProtKB:Q8BMB3][1] [2] [3] [4] Publication Abstract from PubMedA fundamental question in biology is how vertebrates evolved and differ from invertebrates, and little is known about differences in the regulation of translation in the two systems. Herein, we identify a threonyl-tRNA synthetase (TRS)-mediated translation initiation machinery that specifically interacts with eIF4E homologous protein, and forms machinery that is structurally analogous to the eIF4F-mediated translation initiation machinery via the recruitment of other translation initiation components. Biochemical and RNA immunoprecipitation analyses coupled to sequencing suggest that this machinery emerged as a gain-of-function event in the vertebrate lineage, and it positively regulates the translation of mRNAs required for vertebrate development. Collectively, our findings demonstrate that TRS evolved to regulate vertebrate translation initiation via its dual role as a scaffold for the assembly of initiation components and as a selector of target mRNAs. This work highlights the functional significance of aminoacyl-tRNA synthetases in the emergence and control of higher order organisms. A threonyl-tRNA synthetase-mediated translation initiation machinery.,Jeong SJ, Park S, Nguyen LT, Hwang J, Lee EY, Giong HK, Lee JS, Yoon I, Lee JH, Kim JH, Kim HK, Kim D, Yang WS, Kim SY, Lee CY, Yu K, Sonenberg N, Kim MH, Kim S Nat Commun. 2019 Mar 22;10(1):1357. doi: 10.1038/s41467-019-09086-0. PMID:30902983[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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