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Revisiting tRNA chaperones: new players in an ancient game

tRNAs undergo an extensive maturation process including posttranscriptional modifications that influence secondary and tertiary interactions. Precursor and mature tRNAs lacking key modifications are often recognized as aberrant and subsequently targeted for decay, illustrating the importance of modi...

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Detalles Bibliográficos
Autores principales: Porat, Jennifer, Kothe, Ute, Bayfield, Mark A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8051267/
https://www.ncbi.nlm.nih.gov/pubmed/33593999
http://dx.doi.org/10.1261/rna.078428.120
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author Porat, Jennifer
Kothe, Ute
Bayfield, Mark A.
author_facet Porat, Jennifer
Kothe, Ute
Bayfield, Mark A.
author_sort Porat, Jennifer
collection PubMed
description tRNAs undergo an extensive maturation process including posttranscriptional modifications that influence secondary and tertiary interactions. Precursor and mature tRNAs lacking key modifications are often recognized as aberrant and subsequently targeted for decay, illustrating the importance of modifications in promoting structural integrity. tRNAs also rely on tRNA chaperones to promote the folding of misfolded substrates into functional conformations. The best characterized tRNA chaperone is the La protein, which interacts with nascent RNA polymerase III transcripts to promote folding and offers protection from exonucleases. More recently, certain tRNA modification enzymes have also been demonstrated to possess tRNA folding activity distinct from their catalytic activity, suggesting that they may act as tRNA chaperones. In this review, we will discuss pioneering studies relating posttranscriptional modification to tRNA stability and decay pathways, present recent advances into the mechanism by which the RNA chaperone La assists pre-tRNA maturation, and summarize emerging research directions aimed at characterizing modification enzymes as tRNA chaperones. Together, these findings shed light on the importance of tRNA folding and how tRNA chaperones, in particular, increase the fraction of nascent pre-tRNAs that adopt a folded, functional conformation.
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spelling pubmed-80512672021-05-01 Revisiting tRNA chaperones: new players in an ancient game Porat, Jennifer Kothe, Ute Bayfield, Mark A. RNA Review tRNAs undergo an extensive maturation process including posttranscriptional modifications that influence secondary and tertiary interactions. Precursor and mature tRNAs lacking key modifications are often recognized as aberrant and subsequently targeted for decay, illustrating the importance of modifications in promoting structural integrity. tRNAs also rely on tRNA chaperones to promote the folding of misfolded substrates into functional conformations. The best characterized tRNA chaperone is the La protein, which interacts with nascent RNA polymerase III transcripts to promote folding and offers protection from exonucleases. More recently, certain tRNA modification enzymes have also been demonstrated to possess tRNA folding activity distinct from their catalytic activity, suggesting that they may act as tRNA chaperones. In this review, we will discuss pioneering studies relating posttranscriptional modification to tRNA stability and decay pathways, present recent advances into the mechanism by which the RNA chaperone La assists pre-tRNA maturation, and summarize emerging research directions aimed at characterizing modification enzymes as tRNA chaperones. Together, these findings shed light on the importance of tRNA folding and how tRNA chaperones, in particular, increase the fraction of nascent pre-tRNAs that adopt a folded, functional conformation. Cold Spring Harbor Laboratory Press 2021-05 /pmc/articles/PMC8051267/ /pubmed/33593999 http://dx.doi.org/10.1261/rna.078428.120 Text en © 2021 Porat et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society https://creativecommons.org/licenses/by-nc/4.0/This article, published in RNA, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) .
spellingShingle Review
Porat, Jennifer
Kothe, Ute
Bayfield, Mark A.
Revisiting tRNA chaperones: new players in an ancient game
title Revisiting tRNA chaperones: new players in an ancient game
title_full Revisiting tRNA chaperones: new players in an ancient game
title_fullStr Revisiting tRNA chaperones: new players in an ancient game
title_full_unstemmed Revisiting tRNA chaperones: new players in an ancient game
title_short Revisiting tRNA chaperones: new players in an ancient game
title_sort revisiting trna chaperones: new players in an ancient game
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8051267/
https://www.ncbi.nlm.nih.gov/pubmed/33593999
http://dx.doi.org/10.1261/rna.078428.120
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