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A tRNA's fate is decided at its 3' end: Collaborative actions of CCA-adding enzyme and RNases involved in tRNA processing and degradation.

Authors
  • Wellner, Karolin1
  • Betat, Heike1
  • Mörl, Mario2
  • 1 Institute for Biochemistry, Leipzig University, Brüderstr. 34, 04103 Leipzig, Germany. , (Germany)
  • 2 Institute for Biochemistry, Leipzig University, Brüderstr. 34, 04103 Leipzig, Germany. Electronic address: [email protected] , (Germany)
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Apr 01, 2018
Volume
1861
Issue
4
Pages
433–441
Identifiers
DOI: 10.1016/j.bbagrm.2018.01.012
PMID: 29374586
Source
Medline
Keywords
License
Unknown

Abstract

tRNAs are key players in translation and are additionally involved in a wide range of distinct cellular processes. The vital importance of tRNAs becomes evident in numerous diseases that are linked to defective tRNA molecules. It is therefore not surprising that the structural intactness of tRNAs is continuously scrutinized and defective tRNAs are eliminated. In this process, erroneous tRNAs are tagged with single-stranded RNA sequences that are recognized by degrading exonucleases. Recent discoveries have revealed that the CCA-adding enzyme - actually responsible for the de novo synthesis of the 3'-CCA end - plays an indispensable role in tRNA quality control by incorporating a second CCA triplet that is recognized as a degradation tag. In this review, we give an update on the latest findings regarding tRNA quality control that turns out to represent an interplay of the CCA-adding enzyme and RNases involved in tRNA degradation and maturation. In particular, the RNase-induced turnover of the CCA end is now recognized as a trigger for the CCA-adding enzyme to repeatedly scrutinize the structural intactness of a tRNA. This article is part of a Special Issue entitled: SI: Regulation of tRNA synthesis and modification in physiological conditions and disease edited by Dr. Boguta Magdalena.

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