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Polyadenylation helps regulate functional tRNA levels in Escherichia coli

Here we demonstrate a new regulatory mechanism for tRNA processing in Escherichia coli whereby RNase T and RNase PH, the two primary 3′ → 5′ exonucleases involved in the final step of 3′-end maturation, compete with poly(A) polymerase I (PAP I) for tRNA precursors in wild-type cells. In the absence...

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Autores principales: Mohanty, Bijoy K., Maples, Valerie F., Kushner, Sidney R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3378859/
https://www.ncbi.nlm.nih.gov/pubmed/22287637
http://dx.doi.org/10.1093/nar/gks006
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author Mohanty, Bijoy K.
Maples, Valerie F.
Kushner, Sidney R.
author_facet Mohanty, Bijoy K.
Maples, Valerie F.
Kushner, Sidney R.
author_sort Mohanty, Bijoy K.
collection PubMed
description Here we demonstrate a new regulatory mechanism for tRNA processing in Escherichia coli whereby RNase T and RNase PH, the two primary 3′ → 5′ exonucleases involved in the final step of 3′-end maturation, compete with poly(A) polymerase I (PAP I) for tRNA precursors in wild-type cells. In the absence of both RNase T and RNase PH, there is a >30-fold increase of PAP I-dependent poly(A) tails that are ≤10 nt in length coupled with a 2.3- to 4.2-fold decrease in the level of aminoacylated tRNAs and a >2-fold decrease in growth rate. Only 7 out of 86 tRNAs are not regulated by this mechanism and are also not substrates for RNase T, RNase PH or PAP I. Surprisingly, neither PNPase nor RNase II has any effect on tRNA poly(A) tail length. Our data suggest that the polyadenylation of tRNAs by PAP I likely proceeds in a distributive fashion unlike what is observed with mRNAs.
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spelling pubmed-33788592012-06-20 Polyadenylation helps regulate functional tRNA levels in Escherichia coli Mohanty, Bijoy K. Maples, Valerie F. Kushner, Sidney R. Nucleic Acids Res Nucleic Acid Enzymes Here we demonstrate a new regulatory mechanism for tRNA processing in Escherichia coli whereby RNase T and RNase PH, the two primary 3′ → 5′ exonucleases involved in the final step of 3′-end maturation, compete with poly(A) polymerase I (PAP I) for tRNA precursors in wild-type cells. In the absence of both RNase T and RNase PH, there is a >30-fold increase of PAP I-dependent poly(A) tails that are ≤10 nt in length coupled with a 2.3- to 4.2-fold decrease in the level of aminoacylated tRNAs and a >2-fold decrease in growth rate. Only 7 out of 86 tRNAs are not regulated by this mechanism and are also not substrates for RNase T, RNase PH or PAP I. Surprisingly, neither PNPase nor RNase II has any effect on tRNA poly(A) tail length. Our data suggest that the polyadenylation of tRNAs by PAP I likely proceeds in a distributive fashion unlike what is observed with mRNAs. Oxford University Press 2012-05 2012-01-28 /pmc/articles/PMC3378859/ /pubmed/22287637 http://dx.doi.org/10.1093/nar/gks006 Text en © The Author(s) 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Nucleic Acid Enzymes
Mohanty, Bijoy K.
Maples, Valerie F.
Kushner, Sidney R.
Polyadenylation helps regulate functional tRNA levels in Escherichia coli
title Polyadenylation helps regulate functional tRNA levels in Escherichia coli
title_full Polyadenylation helps regulate functional tRNA levels in Escherichia coli
title_fullStr Polyadenylation helps regulate functional tRNA levels in Escherichia coli
title_full_unstemmed Polyadenylation helps regulate functional tRNA levels in Escherichia coli
title_short Polyadenylation helps regulate functional tRNA levels in Escherichia coli
title_sort polyadenylation helps regulate functional trna levels in escherichia coli
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3378859/
https://www.ncbi.nlm.nih.gov/pubmed/22287637
http://dx.doi.org/10.1093/nar/gks006
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