C2-methyladenosine in tRNA promotes protein translation by facilitating the decoding of tandem m2A-tRNA-dependent codons
RNA modification C 2 -methyladenosine (m 2 A) exists in both rRNA and tRNA of Escherichia coli ( E. coli ), installed by the methyltransferase RlmN using a radical- S -adenosylmethionine (SAM) mechanism. However, the precise function of m 2 A in tRNA and its ubiquity in plants have remained unclear....
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| Veröffentlicht in: | Nature communications 2024-02, Vol.15 (1), p.1025-1025, Article 1025 |
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| creator | Duan, Hong-Chao Zhang, Chi Song, Peizhe Yang, Junbo Wang, Ye Jia, Guifang |
| description | RNA modification
C
2
-methyladenosine (m
2
A) exists in both rRNA and tRNA of
Escherichia coli
(
E. coli
), installed by the methyltransferase RlmN using a radical-
S
-adenosylmethionine (SAM) mechanism. However, the precise function of m
2
A in tRNA and its ubiquity in plants have remained unclear. Here we discover the presence of m
2
A in chloroplast rRNA and tRNA, as well as cytosolic tRNA, in multiple plant species. We identify six m
2
A-modified chloroplast tRNAs and two m
2
A-modified cytosolic tRNAs across different plants. Furthermore, we characterize three Arabidopsis m
2
A methyltransferases—RLMNL1, RLMNL2, and RLMNL3—which methylate chloroplast rRNA, chloroplast tRNA, and cytosolic tRNA, respectively. Our findings demonstrate that m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency in chloroplast and cytosol by facilitating decoding of tandem m
2
A-tRNA-dependent codons. This study provides insights into the molecular function and biological significance of m
2
A, uncovering a layer of translation regulation in plants.
Duan et al. demonstrate that the m
2
A modification is ubiquitous in plants and tRNA m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency by facilitating decoding of tandem m
2
A-tRNA-dependent codons. |
| doi_str_mv | 10.1038/s41467-024-45166-6 |
| format | Article |
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C
2
-methyladenosine (m
2
A) exists in both rRNA and tRNA of
Escherichia coli
(
E. coli
), installed by the methyltransferase RlmN using a radical-
S
-adenosylmethionine (SAM) mechanism. However, the precise function of m
2
A in tRNA and its ubiquity in plants have remained unclear. Here we discover the presence of m
2
A in chloroplast rRNA and tRNA, as well as cytosolic tRNA, in multiple plant species. We identify six m
2
A-modified chloroplast tRNAs and two m
2
A-modified cytosolic tRNAs across different plants. Furthermore, we characterize three Arabidopsis m
2
A methyltransferases—RLMNL1, RLMNL2, and RLMNL3—which methylate chloroplast rRNA, chloroplast tRNA, and cytosolic tRNA, respectively. Our findings demonstrate that m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency in chloroplast and cytosol by facilitating decoding of tandem m
2
A-tRNA-dependent codons. This study provides insights into the molecular function and biological significance of m
2
A, uncovering a layer of translation regulation in plants.
Duan et al. demonstrate that the m
2
A modification is ubiquitous in plants and tRNA m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency by facilitating decoding of tandem m
2
A-tRNA-dependent codons.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/s41467-024-45166-6</identifier><identifier>PMID: 38310199</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>140/58 ; 38/91 ; 45/29 ; 49/90 ; 631/337/1645 ; 631/337/574/1793 ; 631/449/1659 ; 631/45/2783 ; Chloroplasts ; Codons ; Cytosol ; E coli ; Escherichia coli ; Humanities and Social Sciences ; Methyltransferase ; multidisciplinary ; Plant species ; RNA modification ; rRNA ; S-Adenosylmethionine ; Science ; Science (multidisciplinary) ; Transfer RNA ; Translation ; tRNA ; tRNA Ala</subject><ispartof>Nature communications, 2024-02, Vol.15 (1), p.1025-1025, Article 1025</ispartof><rights>The Author(s) 2024</rights><rights>The Author(s) 2024. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-cde094ab3f8fc4b9062304ef729ebe38efacc72f36106a507651f047febaa353</citedby><cites>FETCH-LOGICAL-c382t-cde094ab3f8fc4b9062304ef729ebe38efacc72f36106a507651f047febaa353</cites><orcidid>0000-0002-4186-6922 ; 0000-0002-5827-6021</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10838301/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10838301/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids></links><search><creatorcontrib>Duan, Hong-Chao</creatorcontrib><creatorcontrib>Zhang, Chi</creatorcontrib><creatorcontrib>Song, Peizhe</creatorcontrib><creatorcontrib>Yang, Junbo</creatorcontrib><creatorcontrib>Wang, Ye</creatorcontrib><creatorcontrib>Jia, Guifang</creatorcontrib><title>C2-methyladenosine in tRNA promotes protein translation by facilitating the decoding of tandem m2A-tRNA-dependent codons</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><description>RNA modification
C
2
-methyladenosine (m
2
A) exists in both rRNA and tRNA of
Escherichia coli
(
E. coli
), installed by the methyltransferase RlmN using a radical-
S
-adenosylmethionine (SAM) mechanism. However, the precise function of m
2
A in tRNA and its ubiquity in plants have remained unclear. Here we discover the presence of m
2
A in chloroplast rRNA and tRNA, as well as cytosolic tRNA, in multiple plant species. We identify six m
2
A-modified chloroplast tRNAs and two m
2
A-modified cytosolic tRNAs across different plants. Furthermore, we characterize three Arabidopsis m
2
A methyltransferases—RLMNL1, RLMNL2, and RLMNL3—which methylate chloroplast rRNA, chloroplast tRNA, and cytosolic tRNA, respectively. Our findings demonstrate that m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency in chloroplast and cytosol by facilitating decoding of tandem m
2
A-tRNA-dependent codons. This study provides insights into the molecular function and biological significance of m
2
A, uncovering a layer of translation regulation in plants.
Duan et al. demonstrate that the m
2
A modification is ubiquitous in plants and tRNA m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency by facilitating decoding of tandem m
2
A-tRNA-dependent codons.</description><subject>140/58</subject><subject>38/91</subject><subject>45/29</subject><subject>49/90</subject><subject>631/337/1645</subject><subject>631/337/574/1793</subject><subject>631/449/1659</subject><subject>631/45/2783</subject><subject>Chloroplasts</subject><subject>Codons</subject><subject>Cytosol</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Humanities and Social Sciences</subject><subject>Methyltransferase</subject><subject>multidisciplinary</subject><subject>Plant species</subject><subject>RNA modification</subject><subject>rRNA</subject><subject>S-Adenosylmethionine</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Transfer RNA</subject><subject>Translation</subject><subject>tRNA</subject><subject>tRNA 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modification</topic><topic>rRNA</topic><topic>S-Adenosylmethionine</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Transfer RNA</topic><topic>Translation</topic><topic>tRNA</topic><topic>tRNA Ala</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Duan, Hong-Chao</creatorcontrib><creatorcontrib>Zhang, Chi</creatorcontrib><creatorcontrib>Song, Peizhe</creatorcontrib><creatorcontrib>Yang, Junbo</creatorcontrib><creatorcontrib>Wang, Ye</creatorcontrib><creatorcontrib>Jia, Guifang</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full 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Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Duan, Hong-Chao</au><au>Zhang, Chi</au><au>Song, Peizhe</au><au>Yang, Junbo</au><au>Wang, Ye</au><au>Jia, Guifang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>C2-methyladenosine in tRNA promotes protein translation by facilitating the decoding of tandem m2A-tRNA-dependent codons</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><date>2024-02-03</date><risdate>2024</risdate><volume>15</volume><issue>1</issue><spage>1025</spage><epage>1025</epage><pages>1025-1025</pages><artnum>1025</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>RNA modification
C
2
-methyladenosine (m
2
A) exists in both rRNA and tRNA of
Escherichia coli
(
E. coli
), installed by the methyltransferase RlmN using a radical-
S
-adenosylmethionine (SAM) mechanism. However, the precise function of m
2
A in tRNA and its ubiquity in plants have remained unclear. Here we discover the presence of m
2
A in chloroplast rRNA and tRNA, as well as cytosolic tRNA, in multiple plant species. We identify six m
2
A-modified chloroplast tRNAs and two m
2
A-modified cytosolic tRNAs across different plants. Furthermore, we characterize three Arabidopsis m
2
A methyltransferases—RLMNL1, RLMNL2, and RLMNL3—which methylate chloroplast rRNA, chloroplast tRNA, and cytosolic tRNA, respectively. Our findings demonstrate that m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency in chloroplast and cytosol by facilitating decoding of tandem m
2
A-tRNA-dependent codons. This study provides insights into the molecular function and biological significance of m
2
A, uncovering a layer of translation regulation in plants.
Duan et al. demonstrate that the m
2
A modification is ubiquitous in plants and tRNA m
2
A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency by facilitating decoding of tandem m
2
A-tRNA-dependent codons.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>38310199</pmid><doi>10.1038/s41467-024-45166-6</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-4186-6922</orcidid><orcidid>https://orcid.org/0000-0002-5827-6021</orcidid><oa>free_for_read</oa></addata></record> |
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| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10838301 |
| source | DOAJ Directory of Open Access Journals; Springer Nature OA Free Journals; Nature Free; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | 140/58 38/91 45/29 49/90 631/337/1645 631/337/574/1793 631/449/1659 631/45/2783 Chloroplasts Codons Cytosol E coli Escherichia coli Humanities and Social Sciences Methyltransferase multidisciplinary Plant species RNA modification rRNA S-Adenosylmethionine Science Science (multidisciplinary) Transfer RNA Translation tRNA tRNA Ala |
| title | C2-methyladenosine in tRNA promotes protein translation by facilitating the decoding of tandem m2A-tRNA-dependent codons |
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