Determination of the minimal fragment of the poliovirus IRES that is necessary for the formation of a specific complex with the human glycyl-tRNA synthetase

Nikonova, E. Yu.; Mihaylina, A. O.; Lekontseva, N.V.; Nikonov, Oleg; Klyashtorny, V. G.; Кравченко, О. В.; Andreev, Dmitry E.; Shatsky, Ivan N.; Garber, Maria

doi:10.1134/s0006350916020135

Cited by 6 publications

(2 citation statements)

References 19 publications

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“…In vitro binding assays revealed that GlyRS binds an anticodon‐mimic within the poliovirus IRES. Further, GlyRS association was significantly reduced upon deletion of the anticodon‐mimic from the IRES (Andreev et al, ; Nikonova et al, ). Intriguingly, the anticodon‐mimic contains an ACC anticodon‐like triplet, which corresponds to a tRNA Gly that does not exist in human.…”

Section: Aars Functions Outside Of Trna Chargingmentioning

confidence: 99%

RNA mimicry in post‐transcriptional regulation by aminoacyl tRNA synthetases

2019

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Aminoacyl tRNA synthetases (aaRS) are well studied for their roles in tRNA charging with cognate amino acid. Nevertheless, numerous lines of evidence indicate that these proteins have roles other than tRNA charging. These include coordination of cellular signaling cascades, induction of cytokines outside the cell and transcription regulation. Herein, we focus on their roles in post‐transcriptional regulation of mRNA expression. We describe functions that are related to antitermination of transcription, RNA splicing and mRNA translation. Cases were recognition of mRNA by the aaRS involves recognition of tRNA‐like structures are described. Such recognition may be achieved by repurposing tRNA‐binding domains or through domains added to the aaRS later in evolution. Furthermore, we describe cases in which binding by aaRS is implicated in autogenous regulation of expression. Overall, we propose RNA‐mimicry as a common mode of interaction between aaRS and mRNA which allows efficient expression regulation. This article is categorized under: RNA Processing > tRNA Processing RNA Interactions with Proteins and Other Molecules > Protein–RNA Recognition RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications Translation > Translation Regulation

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Section: Aars Functions Outside Of Trna Chargingmentioning

confidence: 99%

RNA mimicry in post‐transcriptional regulation by aminoacyl tRNA synthetases

2019

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“…Some of such functions are linked to tRNA mimicry elements exploited by some viral RNAs [ 66 ]. We previously demonstrated that one of the tRNA synthetases, GARS, selectively and efficiently binds to the apical part of domain V of the poliovirus IRES element which contains a “gly-anticodon stem-loop” mimicry element [ 67 , 68 ]. Notably, this element is evolutionarily conserved in perhaps all type-I IRES containing viruses [ 67 , 69 ].…”

Section: Introductionmentioning

confidence: 99%

Elusive Trans-Acting Factors Which Operate with Type I (Poliovirus-like) IRES Elements

Andreev

Niepmann²,

Shatsky³

2022

IJMS

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The phenomenon of internal initiation of translation was discovered in 1988 on poliovirus mRNA. The prototypic cis-acting element in the 5′ untranslated region (5′UTR) of poliovirus mRNA, which is able to direct initiation at an internal start codon without the involvement of a cap structure, has been called an IRES (Internal Ribosome Entry Site or Segment). Despite its early discovery, poliovirus and other related IRES elements of type I are poorly characterized, and it is not yet clear which host proteins (a.k.a. IRES trans-acting factors, ITAFs) are required for their full activity in vivo. Here we discuss recent and old results devoted to type I IRESes and provide evidence that Poly(rC) binding protein 2 (PCBP2), Glycyl-tRNA synthetase (GARS), and Cold Shock Domain Containing E1 (CSDE1, also known as UNR) are major regulators of type I IRES activity.

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