Glycyl-tRNA Synthetase as a Potential Universal Regulator of Translation Initiation at IRES-I

Nikonova, E. Yu.; Mihaylina, A. O.; Nemchinova, Mariia; Garber, Maria; Nikonov, Oleg

doi:10.1134/s0026893318010156

Cited by 3 publications

(2 citation statements)

References 19 publications

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“…Recently, in vitro studies revealed that human GlyRS can also bind IRESs from other viruses, which are likely to contain an anticodon‐like structure. Interestingly, these studies also suggested a homodimer binding of GlyRS to this structure (Nikonova, Mihaylina, Nemchinova, Garber, & Nikonov, ). Thus, binding to IRES elements is conserved among other viruses in regard to both target sequence and interaction mode.…”

Section: Aars Functions Outside Of Trna Chargingmentioning

confidence: 84%

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: 84%

RNA mimicry in post‐transcriptional regulation by aminoacyl tRNA synthetases

2019

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“…Sixteen nucleotides (underlined) at the 5′-end of oligo RNAs and miRNAs were added to increase the accessibility of short RNA fragments for interaction with proteins. As a negative control, biotinylated tRNA Gly and IRES element mRNA ( Figure 1 ) were obtained as described [ 58 , 59 , 60 ]. Biotinylated RNA fragments were applied onto the NLC sensor chips with immobilized avidin (Bio-Rad, Hercules, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

The RNA-Binding and RNA-Melting Activities of the Multifunctional Protein Nucleobindin 1

Mikhaylina

Svoeglazova

Stolboushkina

et al. 2023

IJMS

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Nucleobindin 1 (NUCB1) is a ubiquitous multidomain protein that belongs to the EF-hand Ca2+-binding superfamily. NUCB1 interacts with Galphai3 protein, cyclooxygenase, amyloid precursor protein, and lipids. It is involved in stress response and human diseases. In addition, this protein is a transcription factor that binds to the DNA E-box motif. Using surface plasmon resonance and molecular beacon approaches, we first showed the RNA binding and RNA melting activities of NUCB1. We suggest that NUCB1 could induce local changes in structured RNAs via binding to the GGAUAU loop sequence. Our results demonstrate the importance of the multidomain structure of NUCB1 for its RNA-chaperone activity in vitro.

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