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Review
. 2014 Jun 11:5:171.
doi: 10.3389/fgene.2014.00171. eCollection 2014.

tRNAs as regulators of biological processes

Affiliations
Review

tRNAs as regulators of biological processes

Medha Raina et al. Front Genet. .

Abstract

Transfer RNAs (tRNA) are best known for their role as adaptors during translation of the genetic code. Beyond their canonical role during protein biosynthesis, tRNAs also perform additional functions in both prokaryotes and eukaryotes for example in regulating gene expression. Aminoacylated tRNAs have also been implicated as substrates for non-ribosomal peptide bond formation, post-translational protein labeling, modification of phospholipids in the cell membrane, and antibiotic biosyntheses. Most recently tRNA fragments, or tRFs, have also been recognized to play regulatory roles. Here, we examine in more detail some of the new functions emerging for tRNA in a variety of cellular processes outside of protein synthesis.

Keywords: amino acid; protein synthesis; regulation; transfer RNA; translation.

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Figures

FIGURE 1
FIGURE 1
Various roles of charged and uncharged tRNA in the cell.
FIGURE 2
FIGURE 2
Formation of small RNAs from tRNA. Precursor tRNAs are processed by RNase P, RNase Z, the splicing endonuclease and CCA-adding enzyme to form mature tRNA in the nucleus. Processing of both the pre-tRNA and mature tRNA can give rise to small RNA. The figure shows possible routes for small RNA (tRNA halves, 5′ tRF, 3′ CCA tRF, 3′ U tRF and 5′ leader exon tRF) production from tRNA. The dashed lines and question marks indicate mechanisms of formation or transport of these tRFs that are not clear.
FIGURE 3
FIGURE 3
Intrinsic pathway for apoptosis. The intrinsic pathway, typically initiated by DNA damage activates p53. p53 then activates the pro-apoptotic proteins, which cause mitochondrial outer membrane permeabilization (MOMP) leading to release of cytochrome c into the cytoplasm. In the cytoplasm cytochrome c associates with Apaf-1 to form the apoptosome complex. However, tRNA may interact with cytochrome c and prevent its binding to Apaf-1. The apoptosome causes the conversion of inactive pro-caspase-9 into active caspase-9. Caspase-9 then activates caspase-3 that then leads to the caspase cascade, resulting in apoptosis.

References

    1. Abramochkin G., Shrader T. E. (1996). Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase. J. Biol. Chem. 271 22901–22907 10.1074/jbc.271.37.22901 - DOI - PubMed
    1. Ashkenazi A., Dixit V. M. (1998). Death receptors: signaling and modulation. Science 281 1305–1308 10.1126/science.281.5381.1305 - DOI - PubMed
    1. Babiarz J. E., Ruby J. G., Wang Y., Bartel D. P., Blelloch R. (2008). Mouse ES cells express endogenous shRNAs, siRNAs, and other microprocessor-independent, Dicer-dependent small RNAs. Genes Dev. 22 2773–2785 10.1101/gad.1705308 - DOI - PMC - PubMed
    1. Bachmair A., Finley D., Varshavsky A. (1986). In vivo half-life of a protein is a function of its amino-terminal residue. Science 234 179–186 10.1126/science.3018930 - DOI - PubMed
    1. Banerjee R., Chen S., Dare K., Gilreath M., Praetorius-Ibba M., Raina M., et al. (2010). tRNAs: cellular barcodes for amino acids. FEBS Lett. 584 387–395 10.1016/j.febslet.2009.11.013 - DOI - PMC - PubMed