Abstract
Transfer RNAs (tRNAs) are essential adaptors that mediate translation of the genetic code. These molecules undergo a variety of post-transcriptional modifications, which expand their chemical reactivity while influencing their structure, stability, and functionality. Chemical modifications to tRNA ensure translational competency and promote cellular viability. Hence, the placement and prevalence of tRNA modifications affects the efficiency of aminoacyl tRNA synthetase (aaRS) reactions, interactions with the ribosome, and transient pairing with messenger RNA (mRNA). The synthesis and abundance of tRNA modifications respond directly and indirectly to a range of environmental and nutritional factors involved in the maintenance of metabolic homeostasis. The dynamic landscape of the tRNA epitranscriptome suggests a role for tRNA modifications as markers of cellular status and regulators of translational capacity. This review discusses the non-canonical roles that tRNA modifications play in central metabolic processes and how their levels are modulated in response to a range of cellular demands.
Highlights
Post-transcriptional modifications expand the role of ribonucleic acids (RNAs) by introducing additional chemical functionalities to their associated nucleotides
Over 150 modifications have been discovered in RNA, 93 of which are exclusively found in transfer RNAs [1]
The presence of these modifications, along with the widely conserved 30 -CCA sequence used for aminoacylation, serve as prerequisites for fully functional transfer RNAs (tRNAs) used during protein synthesis [7]
Summary
Post-transcriptional modifications expand the role of ribonucleic acids (RNAs) by introducing additional chemical functionalities to their associated nucleotides. Modifications are present throughout the tRNA structure (Figure 1) and their functions can be predicted based on their locations within the molecule [6]. Thermus aquaticus by their bindingwith interface contacts aminoacylation (m5U54). ProRS and other additional examples in this that interact with their aaRSs,not butonly with essential partners including tRNA-modifying the prevalence of corresponding these modifications impacts the tRNA’s ability to interact with their enzymes, Ef-Tu,aaRSs, ribosomes and with coding. LysRS binding [17]; agm [20]; C34 U35/U36, interacts necessary structural stability interactions with coli PheRS
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