ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding
The m A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m A readers constitute a super family of proteins with hu...
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creator | Seigneurin-Berny, Daphné Karczewski, Claire Delaforge, Elise Yaacoub, Karen Gaspar Litholdo, Jr, Celso Favory, Jean-Jacques Ringkjøbing Jensen, Malene Bousquet-Antonelli, Cécile Verdel, André |
description | The m
A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m
A readers constitute a super family of proteins with hundreds of members that share a so-called YTH RNA binding domain. The majority of YTH proteins carry no obvious additional domain except for an Intrinsically Disordered Region (IDR). In
IDRs are important for the functional specialization among the different YTH proteins, known as Evolutionarily Conserved
-Terminal region, ECT 1 to 12. Here by studying the ECT2 protein and using an
biochemical characterization, we show that full-length ECT2 and its YTH domain alone have a distinct ability to bind m
A, conversely to previously characterized YTH readers. We identify peptide regions outside of ECT2 YTH domain, in the N-terminal IDR, that regulate its binding to m
A-methylated RNA. Furthermore, we show that the selectivity of ECT2 binding for m
A is enhanced by a high uridine content within its neighbouring sequence, where ECT2 N-terminal IDR is believed to contact the target RNA
. Finally, we also identify small structural elements, located next to ECT2 YTH domain and conserved in a large set of YTH proteins, that enhance its binding to m
A-methylated RNA. We propose from these findings that some of these regulatory regions are not limited to ECT2 or YTH readers of flowering plants but may be widespread among eukaryotic YTH readers. |
doi_str_mv | 10.1080/15476286.2024.2399914 |
format | Article |
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A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m
A readers constitute a super family of proteins with hundreds of members that share a so-called YTH RNA binding domain. The majority of YTH proteins carry no obvious additional domain except for an Intrinsically Disordered Region (IDR). In
IDRs are important for the functional specialization among the different YTH proteins, known as Evolutionarily Conserved
-Terminal region, ECT 1 to 12. Here by studying the ECT2 protein and using an
biochemical characterization, we show that full-length ECT2 and its YTH domain alone have a distinct ability to bind m
A, conversely to previously characterized YTH readers. We identify peptide regions outside of ECT2 YTH domain, in the N-terminal IDR, that regulate its binding to m
A-methylated RNA. Furthermore, we show that the selectivity of ECT2 binding for m
A is enhanced by a high uridine content within its neighbouring sequence, where ECT2 N-terminal IDR is believed to contact the target RNA
. Finally, we also identify small structural elements, located next to ECT2 YTH domain and conserved in a large set of YTH proteins, that enhance its binding to m
A-methylated RNA. We propose from these findings that some of these regulatory regions are not limited to ECT2 or YTH readers of flowering plants but may be widespread among eukaryotic YTH readers.</description><identifier>ISSN: 1547-6286</identifier><identifier>EISSN: 1555-8584</identifier><identifier>DOI: 10.1080/15476286.2024.2399914</identifier><identifier>PMID: 39267376</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Adenosine - metabolism ; Amino Acid Sequence ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Binding Sites ; Intracellular Signaling Peptides and Proteins ; Intrinsically Disordered Proteins - chemistry ; Intrinsically Disordered Proteins - genetics ; Intrinsically Disordered Proteins - metabolism ; Life Sciences ; Methylation ; Protein Binding ; Protein Domains ; RNA, Plant - chemistry ; RNA, Plant - genetics ; RNA, Plant - metabolism ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism</subject><ispartof>RNA biology, 2024-12, Vol.21 (1), p.1-958</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c1504-8111c70ed2a5f3936b3adedcc3b9bd389a03e571f24ca700e4d7f09e8f53ad163</cites><orcidid>0000-0001-6048-3794 ; 0000-0002-7436-9885 ; 0000-0002-3909-7976 ; 0000-0003-0419-2196</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,860,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39267376$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04727927$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Seigneurin-Berny, Daphné</creatorcontrib><creatorcontrib>Karczewski, Claire</creatorcontrib><creatorcontrib>Delaforge, Elise</creatorcontrib><creatorcontrib>Yaacoub, Karen</creatorcontrib><creatorcontrib>Gaspar Litholdo, Jr, Celso</creatorcontrib><creatorcontrib>Favory, Jean-Jacques</creatorcontrib><creatorcontrib>Ringkjøbing Jensen, Malene</creatorcontrib><creatorcontrib>Bousquet-Antonelli, Cécile</creatorcontrib><creatorcontrib>Verdel, André</creatorcontrib><title>ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding</title><title>RNA biology</title><addtitle>RNA Biol</addtitle><description>The m
A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m
A readers constitute a super family of proteins with hundreds of members that share a so-called YTH RNA binding domain. The majority of YTH proteins carry no obvious additional domain except for an Intrinsically Disordered Region (IDR). In
IDRs are important for the functional specialization among the different YTH proteins, known as Evolutionarily Conserved
-Terminal region, ECT 1 to 12. Here by studying the ECT2 protein and using an
biochemical characterization, we show that full-length ECT2 and its YTH domain alone have a distinct ability to bind m
A, conversely to previously characterized YTH readers. We identify peptide regions outside of ECT2 YTH domain, in the N-terminal IDR, that regulate its binding to m
A-methylated RNA. Furthermore, we show that the selectivity of ECT2 binding for m
A is enhanced by a high uridine content within its neighbouring sequence, where ECT2 N-terminal IDR is believed to contact the target RNA
. Finally, we also identify small structural elements, located next to ECT2 YTH domain and conserved in a large set of YTH proteins, that enhance its binding to m
A-methylated RNA. We propose from these findings that some of these regulatory regions are not limited to ECT2 or YTH readers of flowering plants but may be widespread among eukaryotic YTH readers.</description><subject>Adenosine - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Intrinsically Disordered Proteins - chemistry</subject><subject>Intrinsically Disordered Proteins - genetics</subject><subject>Intrinsically Disordered Proteins - metabolism</subject><subject>Life Sciences</subject><subject>Methylation</subject><subject>Protein Binding</subject><subject>Protein Domains</subject><subject>RNA, Plant - chemistry</subject><subject>RNA, Plant - genetics</subject><subject>RNA, Plant - metabolism</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><issn>1547-6286</issn><issn>1555-8584</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtKw0AUQAdRbK1-gjJbF6nzfixDqVYIClIXrsIkc9NGmoeZRPDvbehjdS-Xc-7iIHRPyZwSQ56oFFoxo-aMMDFn3FpLxQWaUillZKQRl-MudDRCE3QTwjchXBkrr9GEW6Y012qKkuVizXALbV96wAF-BqhzCLgZ-jBe-i3gr_UK-6ZyZY072Aw71wMu-4ArrHAcfbzFOCtrX9abW3RVuF2Au-Ococ_n5XqxipL3l9dFnEQ5lUREhlKaawKeOVlwy1XGnQef5zyzmefGOsJBalowkTtNCAivC2LBFHIPUsVn6PHwd-t2aduVlev-0saV6SpO0vFGhGbaMv1L96w8sHnXhNBBcRYoSceS6alkOpZMjyX33sPBa4esAn-2Tun4Py3HbBc</recordid><startdate>20241231</startdate><enddate>20241231</enddate><creator>Seigneurin-Berny, Daphné</creator><creator>Karczewski, Claire</creator><creator>Delaforge, Elise</creator><creator>Yaacoub, Karen</creator><creator>Gaspar Litholdo, Jr, Celso</creator><creator>Favory, Jean-Jacques</creator><creator>Ringkjøbing Jensen, Malene</creator><creator>Bousquet-Antonelli, Cécile</creator><creator>Verdel, André</creator><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0001-6048-3794</orcidid><orcidid>https://orcid.org/0000-0002-7436-9885</orcidid><orcidid>https://orcid.org/0000-0002-3909-7976</orcidid><orcidid>https://orcid.org/0000-0003-0419-2196</orcidid></search><sort><creationdate>20241231</creationdate><title>ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding</title><author>Seigneurin-Berny, Daphné ; Karczewski, Claire ; Delaforge, Elise ; Yaacoub, Karen ; Gaspar Litholdo, Jr, Celso ; Favory, Jean-Jacques ; Ringkjøbing Jensen, Malene ; Bousquet-Antonelli, Cécile ; Verdel, André</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1504-8111c70ed2a5f3936b3adedcc3b9bd389a03e571f24ca700e4d7f09e8f53ad163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Adenosine - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Intrinsically Disordered Proteins - chemistry</topic><topic>Intrinsically Disordered Proteins - genetics</topic><topic>Intrinsically Disordered Proteins - metabolism</topic><topic>Life Sciences</topic><topic>Methylation</topic><topic>Protein Binding</topic><topic>Protein Domains</topic><topic>RNA, Plant - chemistry</topic><topic>RNA, Plant - genetics</topic><topic>RNA, Plant - metabolism</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Seigneurin-Berny, Daphné</creatorcontrib><creatorcontrib>Karczewski, Claire</creatorcontrib><creatorcontrib>Delaforge, Elise</creatorcontrib><creatorcontrib>Yaacoub, Karen</creatorcontrib><creatorcontrib>Gaspar Litholdo, Jr, Celso</creatorcontrib><creatorcontrib>Favory, Jean-Jacques</creatorcontrib><creatorcontrib>Ringkjøbing Jensen, Malene</creatorcontrib><creatorcontrib>Bousquet-Antonelli, Cécile</creatorcontrib><creatorcontrib>Verdel, André</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>RNA biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Seigneurin-Berny, Daphné</au><au>Karczewski, Claire</au><au>Delaforge, Elise</au><au>Yaacoub, Karen</au><au>Gaspar Litholdo, Jr, Celso</au><au>Favory, Jean-Jacques</au><au>Ringkjøbing Jensen, Malene</au><au>Bousquet-Antonelli, Cécile</au><au>Verdel, André</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding</atitle><jtitle>RNA biology</jtitle><addtitle>RNA Biol</addtitle><date>2024-12-31</date><risdate>2024</risdate><volume>21</volume><issue>1</issue><spage>1</spage><epage>958</epage><pages>1-958</pages><issn>1547-6286</issn><eissn>1555-8584</eissn><abstract>The m
A epitranscriptomic mark is the most abundant and widespread internal RNA chemical modification, which through the control of RNA acts as an important factor of eukaryote reproduction, growth, morphogenesis and stress response. The main m
A readers constitute a super family of proteins with hundreds of members that share a so-called YTH RNA binding domain. The majority of YTH proteins carry no obvious additional domain except for an Intrinsically Disordered Region (IDR). In
IDRs are important for the functional specialization among the different YTH proteins, known as Evolutionarily Conserved
-Terminal region, ECT 1 to 12. Here by studying the ECT2 protein and using an
biochemical characterization, we show that full-length ECT2 and its YTH domain alone have a distinct ability to bind m
A, conversely to previously characterized YTH readers. We identify peptide regions outside of ECT2 YTH domain, in the N-terminal IDR, that regulate its binding to m
A-methylated RNA. Furthermore, we show that the selectivity of ECT2 binding for m
A is enhanced by a high uridine content within its neighbouring sequence, where ECT2 N-terminal IDR is believed to contact the target RNA
. Finally, we also identify small structural elements, located next to ECT2 YTH domain and conserved in a large set of YTH proteins, that enhance its binding to m
A-methylated RNA. We propose from these findings that some of these regulatory regions are not limited to ECT2 or YTH readers of flowering plants but may be widespread among eukaryotic YTH readers.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>39267376</pmid><doi>10.1080/15476286.2024.2399914</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0001-6048-3794</orcidid><orcidid>https://orcid.org/0000-0002-7436-9885</orcidid><orcidid>https://orcid.org/0000-0002-3909-7976</orcidid><orcidid>https://orcid.org/0000-0003-0419-2196</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine - metabolism Amino Acid Sequence Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Binding Sites Intracellular Signaling Peptides and Proteins Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - genetics Intrinsically Disordered Proteins - metabolism Life Sciences Methylation Protein Binding Protein Domains RNA, Plant - chemistry RNA, Plant - genetics RNA, Plant - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism |
title | ECT2 peptide sequences outside the YTH domain regulate its m 6 A-RNA binding |
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