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. N6-adenosine methyl...

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Authors: Yue, Jianying, Lu, Yan, Sun, Zhenqi, Guo, Yuqing, San León, David, Pasin, Fabio, Zhao, Mingmin
Format: article
Status:Published version
Publication Date:2023
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/363620
Online Access:http://hdl.handle.net/10261/363620
https://api.elsevier.com/content/abstract/scopus_id/85159769610
Access Level:Open access
Keyword:METTL
Methyltransferase
N6-methyladenosine
Potyviridae
RNA virus
antiviral immunity
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spelling Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responsesYue, JianyingLu, YanSun, ZhenqiGuo, YuqingSan León, DavidPasin, FabioZhao, MingminMETTLMethyltransferaseN6-methyladenosinePotyviridaeRNA virusantiviral immunityMethyltransferase (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. N6-adenosine methylation (m6A) is a common chemical modification of eukaryotic and viral RNA whose abundance is jointly regulated by MTases and METTLs, demethylases, and m6A binding proteins. m6A 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.This study was supported by National Science Foundation of China (grants 31770165 and 31860489 to M.Z.) and Major project of Nature Science Foundation of Inner Mongolia of China (grants 2021ZD06 to M. Z.). F.P. is supported by a “Juan de la Cierva Incorporación” contract (IJC2019-039970-I) from Ministerio de Ciencia e Innovación (Spain), and grants MiniVi (ELIXIR-IIB, Cineca, Italy) and BCV-2023-1-0021 (Red Española de Supercomputación, Spain).Peer reviewedTaylor & FrancisSan León, David [0000-0001-8138-500X]Pasin, Fabio [0000-0002-9620-4301]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/363620https://api.elsevier.com/content/abstract/scopus_id/85159769610reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésPlant signaling & behaviorapplication/pdfhttps://www.tandfonline.com/doi/full/10.1080/15592324.2023.2214760Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3636202026-05-22T06:33:51Z
dc.title.none.fl_str_mv Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses
title Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses
spellingShingle Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses
Yue, Jianying
METTL
Methyltransferase
N6-methyladenosine
Potyviridae
RNA virus
antiviral immunity
title_short 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_sort Methyltransferase-like (METTL) homologues participate in Nicotiana benthamiana antiviral responses
dc.creator.none.fl_str_mv Yue, Jianying
Lu, Yan
Sun, Zhenqi
Guo, Yuqing
San León, David
Pasin, Fabio
Zhao, Mingmin
author Yue, Jianying
author_facet Yue, Jianying
Lu, Yan
Sun, Zhenqi
Guo, Yuqing
San León, David
Pasin, Fabio
Zhao, Mingmin
author_role author
author2 Lu, Yan
Sun, Zhenqi
Guo, Yuqing
San León, David
Pasin, Fabio
Zhao, Mingmin
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv San León, David [0000-0001-8138-500X]
Pasin, Fabio [0000-0002-9620-4301]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv METTL
Methyltransferase
N6-methyladenosine
Potyviridae
RNA virus
antiviral immunity
topic METTL
Methyltransferase
N6-methyladenosine
Potyviridae
RNA virus
antiviral immunity
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. N6-adenosine methylation (m6A) is a common chemical modification of eukaryotic and viral RNA whose abundance is jointly regulated by MTases and METTLs, demethylases, and m6A binding proteins. m6A 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.
publishDate 2023
dc.date.none.fl_str_mv 2023
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/363620
https://api.elsevier.com/content/abstract/scopus_id/85159769610
url http://hdl.handle.net/10261/363620
https://api.elsevier.com/content/abstract/scopus_id/85159769610
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Plant signaling & behavior
application/pdf
https://www.tandfonline.com/doi/full/10.1080/15592324.2023.2214760
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869421990320799744
score 15,812455

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