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Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs
Transfer RNA modifications play pivotal roles in protein synthesis. N(6)-threonylcarbamoyladenosine (t(6)A) and its derivatives are modifications found at position 37, 3΄-adjacent to the anticodon, in tRNAs responsible for ANN codons. These modifications are universally conserved in all domains of l...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5389704/ https://www.ncbi.nlm.nih.gov/pubmed/27913733 http://dx.doi.org/10.1093/nar/gkw1120 |
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author | Kang, Byeong-il Miyauchi, Kenjyo Matuszewski, Michal D'Almeida, Gabriel Silveira Rubio, Mary Anne T. Alfonzo, Juan D. Inoue, Kazuki Sakaguchi, Yuriko Suzuki, Takeo Sochacka, Elzbieta Suzuki, Tsutomu |
author_facet | Kang, Byeong-il Miyauchi, Kenjyo Matuszewski, Michal D'Almeida, Gabriel Silveira Rubio, Mary Anne T. Alfonzo, Juan D. Inoue, Kazuki Sakaguchi, Yuriko Suzuki, Takeo Sochacka, Elzbieta Suzuki, Tsutomu |
author_sort | Kang, Byeong-il |
collection | PubMed |
description | Transfer RNA modifications play pivotal roles in protein synthesis. N(6)-threonylcarbamoyladenosine (t(6)A) and its derivatives are modifications found at position 37, 3΄-adjacent to the anticodon, in tRNAs responsible for ANN codons. These modifications are universally conserved in all domains of life. t(6)A and its derivatives have pleiotropic functions in protein synthesis including aminoacylation, decoding and translocation. We previously discovered a cyclic form of t(6)A (ct(6)A) as a chemically labile derivative of t(6)A in tRNAs from bacteria, fungi, plants and protists. Here, we report 2-methylthio cyclic t(6)A (ms(2)ct(6)A), a novel derivative of ct(6)A found in tRNAs from Bacillus subtilis, plants and Trypanosoma brucei. In B. subtilis and T. brucei, ms(2)ct(6)A disappeared and remained to be ms(2)t(6)A and ct(6)A by depletion of tcdA and mtaB homologs, respectively, demonstrating that TcdA and MtaB are responsible for biogenesis of ms(2)ct(6)A. |
format | Online Article Text |
id | pubmed-5389704 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-53897042017-04-24 Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs Kang, Byeong-il Miyauchi, Kenjyo Matuszewski, Michal D'Almeida, Gabriel Silveira Rubio, Mary Anne T. Alfonzo, Juan D. Inoue, Kazuki Sakaguchi, Yuriko Suzuki, Takeo Sochacka, Elzbieta Suzuki, Tsutomu Nucleic Acids Res Gene regulation, Chromatin and Epigenetics Transfer RNA modifications play pivotal roles in protein synthesis. N(6)-threonylcarbamoyladenosine (t(6)A) and its derivatives are modifications found at position 37, 3΄-adjacent to the anticodon, in tRNAs responsible for ANN codons. These modifications are universally conserved in all domains of life. t(6)A and its derivatives have pleiotropic functions in protein synthesis including aminoacylation, decoding and translocation. We previously discovered a cyclic form of t(6)A (ct(6)A) as a chemically labile derivative of t(6)A in tRNAs from bacteria, fungi, plants and protists. Here, we report 2-methylthio cyclic t(6)A (ms(2)ct(6)A), a novel derivative of ct(6)A found in tRNAs from Bacillus subtilis, plants and Trypanosoma brucei. In B. subtilis and T. brucei, ms(2)ct(6)A disappeared and remained to be ms(2)t(6)A and ct(6)A by depletion of tcdA and mtaB homologs, respectively, demonstrating that TcdA and MtaB are responsible for biogenesis of ms(2)ct(6)A. Oxford University Press 2017-02-28 2016-12-02 /pmc/articles/PMC5389704/ /pubmed/27913733 http://dx.doi.org/10.1093/nar/gkw1120 Text en © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Gene regulation, Chromatin and Epigenetics Kang, Byeong-il Miyauchi, Kenjyo Matuszewski, Michal D'Almeida, Gabriel Silveira Rubio, Mary Anne T. Alfonzo, Juan D. Inoue, Kazuki Sakaguchi, Yuriko Suzuki, Takeo Sochacka, Elzbieta Suzuki, Tsutomu Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs |
title | Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs |
title_full | Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs |
title_fullStr | Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs |
title_full_unstemmed | Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs |
title_short | Identification of 2-methylthio cyclic N(6)-threonylcarbamoyladenosine (ms(2)ct(6)A) as a novel RNA modification at position 37 of tRNAs |
title_sort | identification of 2-methylthio cyclic n(6)-threonylcarbamoyladenosine (ms(2)ct(6)a) as a novel rna modification at position 37 of trnas |
topic | Gene regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5389704/ https://www.ncbi.nlm.nih.gov/pubmed/27913733 http://dx.doi.org/10.1093/nar/gkw1120 |
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