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Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth

Modified nucleosides in tRNAs are critical for protein translation. N(1)-methylguanosine-37 and N(1)-methylinosine-37 in tRNAs, both located at the 3’-adjacent to the anticodon, are formed by Trm5. Here we describe Arabidopsis thaliana AtTRM5 (At3g56120) as a Trm5 ortholog. Attrm5 mutant plants have...

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Autores principales: Guo, Qianqian, Ng, Pei Qin, Shi, Shanshan, Fan, Diwen, Li, Jun, Zhao, Jing, Wang, Hua, David, Rakesh, Mittal, Parul, Do, Trung, Bock, Ralph, Zhao, Ming, Zhou, Wenbin, Searle, Iain
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6874348/
https://www.ncbi.nlm.nih.gov/pubmed/31756231
http://dx.doi.org/10.1371/journal.pone.0225064
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author Guo, Qianqian
Ng, Pei Qin
Shi, Shanshan
Fan, Diwen
Li, Jun
Zhao, Jing
Wang, Hua
David, Rakesh
Mittal, Parul
Do, Trung
Bock, Ralph
Zhao, Ming
Zhou, Wenbin
Searle, Iain
author_facet Guo, Qianqian
Ng, Pei Qin
Shi, Shanshan
Fan, Diwen
Li, Jun
Zhao, Jing
Wang, Hua
David, Rakesh
Mittal, Parul
Do, Trung
Bock, Ralph
Zhao, Ming
Zhou, Wenbin
Searle, Iain
author_sort Guo, Qianqian
collection PubMed
description Modified nucleosides in tRNAs are critical for protein translation. N(1)-methylguanosine-37 and N(1)-methylinosine-37 in tRNAs, both located at the 3’-adjacent to the anticodon, are formed by Trm5. Here we describe Arabidopsis thaliana AtTRM5 (At3g56120) as a Trm5 ortholog. Attrm5 mutant plants have overall slower growth as observed by slower leaf initiation rate, delayed flowering and reduced primary root length. In Attrm5 mutants, mRNAs of flowering time genes are less abundant and correlated with delayed flowering. We show that AtTRM5 complements the yeast trm5 mutant, and in vitro methylates tRNA guanosine-37 to produce N(1)-methylguanosine (m(1)G). We also show in vitro that AtTRM5 methylates tRNA inosine-37 to produce N(1)-methylinosine (m(1)I) and in Attrm5 mutant plants, we show a reduction of both N(1)-methylguanosine and N(1)-methylinosine. We also show that AtTRM5 is localized to the nucleus in plant cells. Proteomics data showed that photosynthetic protein abundance is affected in Attrm5 mutant plants. Finally, we show tRNA-Ala aminoacylation is not affected in Attrm5 mutants. However the abundance of tRNA-Ala and tRNA-Asp 5’ half cleavage products are deduced. Our findings highlight the bifunctionality of AtTRM5 and the importance of the post-transcriptional tRNA modifications m(1)G and m(1)I at tRNA position 37 in general plant growth and development.
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spelling pubmed-68743482019-12-06 Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth Guo, Qianqian Ng, Pei Qin Shi, Shanshan Fan, Diwen Li, Jun Zhao, Jing Wang, Hua David, Rakesh Mittal, Parul Do, Trung Bock, Ralph Zhao, Ming Zhou, Wenbin Searle, Iain PLoS One Research Article Modified nucleosides in tRNAs are critical for protein translation. N(1)-methylguanosine-37 and N(1)-methylinosine-37 in tRNAs, both located at the 3’-adjacent to the anticodon, are formed by Trm5. Here we describe Arabidopsis thaliana AtTRM5 (At3g56120) as a Trm5 ortholog. Attrm5 mutant plants have overall slower growth as observed by slower leaf initiation rate, delayed flowering and reduced primary root length. In Attrm5 mutants, mRNAs of flowering time genes are less abundant and correlated with delayed flowering. We show that AtTRM5 complements the yeast trm5 mutant, and in vitro methylates tRNA guanosine-37 to produce N(1)-methylguanosine (m(1)G). We also show in vitro that AtTRM5 methylates tRNA inosine-37 to produce N(1)-methylinosine (m(1)I) and in Attrm5 mutant plants, we show a reduction of both N(1)-methylguanosine and N(1)-methylinosine. We also show that AtTRM5 is localized to the nucleus in plant cells. Proteomics data showed that photosynthetic protein abundance is affected in Attrm5 mutant plants. Finally, we show tRNA-Ala aminoacylation is not affected in Attrm5 mutants. However the abundance of tRNA-Ala and tRNA-Asp 5’ half cleavage products are deduced. Our findings highlight the bifunctionality of AtTRM5 and the importance of the post-transcriptional tRNA modifications m(1)G and m(1)I at tRNA position 37 in general plant growth and development. Public Library of Science 2019-11-22 /pmc/articles/PMC6874348/ /pubmed/31756231 http://dx.doi.org/10.1371/journal.pone.0225064 Text en © 2019 Guo et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Guo, Qianqian
Ng, Pei Qin
Shi, Shanshan
Fan, Diwen
Li, Jun
Zhao, Jing
Wang, Hua
David, Rakesh
Mittal, Parul
Do, Trung
Bock, Ralph
Zhao, Ming
Zhou, Wenbin
Searle, Iain
Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
title Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
title_full Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
title_fullStr Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
title_full_unstemmed Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
title_short Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
title_sort arabidopsis trm5 encodes a nuclear-localised bifunctional trna guanine and inosine-n1-methyltransferase that is important for growth
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6874348/
https://www.ncbi.nlm.nih.gov/pubmed/31756231
http://dx.doi.org/10.1371/journal.pone.0225064
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