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Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism

In eukaryotes, almost all RNA species are processed at their 3′ ends and most mRNAs are polyadenylated in the nucleus by canonical poly(A) polymerases. In recent years, several terminal nucleotidyl transferases (TENTs) including non-canonical poly(A) polymerases (ncPAPs) and terminal uridyl transfer...

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Autores principales: Warkocki, Zbigniew, Liudkovska, Vladyslava, Gewartowska, Olga, Mroczek, Seweryn, Dziembowski, Andrzej
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6232586/
https://www.ncbi.nlm.nih.gov/pubmed/30397099
http://dx.doi.org/10.1098/rstb.2018.0162
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author Warkocki, Zbigniew
Liudkovska, Vladyslava
Gewartowska, Olga
Mroczek, Seweryn
Dziembowski, Andrzej
author_facet Warkocki, Zbigniew
Liudkovska, Vladyslava
Gewartowska, Olga
Mroczek, Seweryn
Dziembowski, Andrzej
author_sort Warkocki, Zbigniew
collection PubMed
description In eukaryotes, almost all RNA species are processed at their 3′ ends and most mRNAs are polyadenylated in the nucleus by canonical poly(A) polymerases. In recent years, several terminal nucleotidyl transferases (TENTs) including non-canonical poly(A) polymerases (ncPAPs) and terminal uridyl transferases (TUTases) have been discovered. In contrast to canonical polymerases, TENTs' functions are more diverse; some, especially TUTases, induce RNA decay while others, such as cytoplasmic ncPAPs, activate translationally dormant deadenylated mRNAs. The mammalian genome encodes 11 different TENTs. This review summarizes the current knowledge about the functions and mechanisms of action of these enzymes. This article is part of the theme issue ‘5′ and 3′ modifications controlling RNA degradation’.
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spelling pubmed-62325862018-11-20 Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism Warkocki, Zbigniew Liudkovska, Vladyslava Gewartowska, Olga Mroczek, Seweryn Dziembowski, Andrzej Philos Trans R Soc Lond B Biol Sci Articles In eukaryotes, almost all RNA species are processed at their 3′ ends and most mRNAs are polyadenylated in the nucleus by canonical poly(A) polymerases. In recent years, several terminal nucleotidyl transferases (TENTs) including non-canonical poly(A) polymerases (ncPAPs) and terminal uridyl transferases (TUTases) have been discovered. In contrast to canonical polymerases, TENTs' functions are more diverse; some, especially TUTases, induce RNA decay while others, such as cytoplasmic ncPAPs, activate translationally dormant deadenylated mRNAs. The mammalian genome encodes 11 different TENTs. This review summarizes the current knowledge about the functions and mechanisms of action of these enzymes. This article is part of the theme issue ‘5′ and 3′ modifications controlling RNA degradation’. The Royal Society 2018-12-19 2018-11-05 /pmc/articles/PMC6232586/ /pubmed/30397099 http://dx.doi.org/10.1098/rstb.2018.0162 Text en © 2018 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Articles
Warkocki, Zbigniew
Liudkovska, Vladyslava
Gewartowska, Olga
Mroczek, Seweryn
Dziembowski, Andrzej
Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
title Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
title_full Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
title_fullStr Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
title_full_unstemmed Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
title_short Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
title_sort terminal nucleotidyl transferases (tents) in mammalian rna metabolism
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6232586/
https://www.ncbi.nlm.nih.gov/pubmed/30397099
http://dx.doi.org/10.1098/rstb.2018.0162
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