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Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses
Methyltransferase (MTase) enzymes catalyze the addition of a methyl group to a variety of biological substrates. MTase-like (METTL) proteins are Class I MTases whose enzymatic activities contribute to the epigenetic and epitranscriptomic regulation of multiple cellular processes. N(6)-adenosine meth...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10202045/ https://www.ncbi.nlm.nih.gov/pubmed/37210738 http://dx.doi.org/10.1080/15592324.2023.2214760 |
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author | Yue, Jianying Lu, Yan Sun, Zhenqi Guo, Yuqing San León, David Pasin, Fabio Zhao, Mingmin |
author_facet | Yue, Jianying Lu, Yan Sun, Zhenqi Guo, Yuqing San León, David Pasin, Fabio Zhao, Mingmin |
author_sort | Yue, Jianying |
collection | PubMed |
description | Methyltransferase (MTase) enzymes catalyze the addition of a methyl group to a variety of biological substrates. MTase-like (METTL) proteins are Class I MTases whose enzymatic activities contribute to the epigenetic and epitranscriptomic regulation of multiple cellular processes. N(6)-adenosine methylation (m(6)A) is a common chemical modification of eukaryotic and viral RNA whose abundance is jointly regulated by MTases and METTLs, demethylases, and m(6)A binding proteins. m(6)A affects various cellular processes including RNA degradation, post-transcriptional processing, and antiviral immunity. Here, we used Nicotiana benthamiana and plum pox virus (PPV), an RNA virus of the Potyviridae family, to investigated the roles of MTases in plant–virus interaction. RNA sequencing analysis identified MTase transcripts that are differentially expressed during PPV infection; among these, accumulation of a METTL gene was significantly downregulated. Two N. benthamiana METTL transcripts (NbMETTL1 and NbMETTL2) were cloned and further characterized. Sequence and structural analyses of the two encoded proteins identified a conserved S-adenosyl methionine (SAM) binding domain, showing they are SAM-dependent MTases phylogenetically related to human METTL16 and Arabidopsis thaliana FIONA1. Overexpression of NbMETTL1 and NbMETTL2 caused a decrease of PPV accumulation. In sum, our results indicate that METTL homologues participate in plant antiviral responses. |
format | Online Article Text |
id | pubmed-10202045 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-102020452023-05-23 Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses Yue, Jianying Lu, Yan Sun, Zhenqi Guo, Yuqing San León, David Pasin, Fabio Zhao, Mingmin Plant Signal Behav Research Paper Methyltransferase (MTase) enzymes catalyze the addition of a methyl group to a variety of biological substrates. MTase-like (METTL) proteins are Class I MTases whose enzymatic activities contribute to the epigenetic and epitranscriptomic regulation of multiple cellular processes. N(6)-adenosine methylation (m(6)A) is a common chemical modification of eukaryotic and viral RNA whose abundance is jointly regulated by MTases and METTLs, demethylases, and m(6)A binding proteins. m(6)A affects various cellular processes including RNA degradation, post-transcriptional processing, and antiviral immunity. Here, we used Nicotiana benthamiana and plum pox virus (PPV), an RNA virus of the Potyviridae family, to investigated the roles of MTases in plant–virus interaction. RNA sequencing analysis identified MTase transcripts that are differentially expressed during PPV infection; among these, accumulation of a METTL gene was significantly downregulated. Two N. benthamiana METTL transcripts (NbMETTL1 and NbMETTL2) were cloned and further characterized. Sequence and structural analyses of the two encoded proteins identified a conserved S-adenosyl methionine (SAM) binding domain, showing they are SAM-dependent MTases phylogenetically related to human METTL16 and Arabidopsis thaliana FIONA1. Overexpression of NbMETTL1 and NbMETTL2 caused a decrease of PPV accumulation. In sum, our results indicate that METTL homologues participate in plant antiviral responses. Taylor & Francis 2023-05-21 /pmc/articles/PMC10202045/ /pubmed/37210738 http://dx.doi.org/10.1080/15592324.2023.2214760 Text en © 2023 The Author(s). Published with license by Taylor & Francis Group, LLC. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent. |
spellingShingle | Research Paper Yue, Jianying Lu, Yan Sun, Zhenqi Guo, Yuqing San León, David Pasin, Fabio Zhao, Mingmin Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses |
title | Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses |
title_full | Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses |
title_fullStr | Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses |
title_full_unstemmed | Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses |
title_short | Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses |
title_sort | methyltransferase-like (mettl) homologues participate in nicotiana benthamiana antiviral responses |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10202045/ https://www.ncbi.nlm.nih.gov/pubmed/37210738 http://dx.doi.org/10.1080/15592324.2023.2214760 |
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