Mapping domains of ARS2 critical for its RNA decay capacity
Abstract ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a de...
Gespeichert in:
Veröffentlicht in: | Nucleic acids research 2020-07, Vol.48 (12), p.6943-6953 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 6953 |
---|---|
container_issue | 12 |
container_start_page | 6943 |
container_title | Nucleic acids research |
container_volume | 48 |
creator | Melko, Mireille Winczura, Kinga Rouvière, Jérôme Olivier Oborská-Oplová, Michaela Andersen, Pia K Heick Jensen, Torben |
description | Abstract
ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a degradation phenotype aided by its interaction with the poly(A) tail exosome targeting (PAXT) connection. Interestingly, C-terminal amino acids of ARS2, responsible for binding the RNA 5′cap binding complex (CBC), become dispensable when ARS2 is directly tethered to the reporter RNA. In contrast, the Zinc-finger (ZnF) domain of ARS2 is essential for the decay of both reporters and consistently co-immunoprecipitation analyses reveal a necessity of this domain for the interaction of ARS2 with the PAXT-associated RNA helicase MTR4. Taken together, our results map the domains of ARS2 underlying two essential properties of the protein: its RNP targeting ability and its capacity to recruit the RNA decay machinery. |
doi_str_mv | 10.1093/nar/gkaa445 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7337933</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1093/nar/gkaa445</oup_id><sourcerecordid>2407579925</sourcerecordid><originalsourceid>FETCH-LOGICAL-c412t-432c468cb2fb61d6f4d2773f27e87b728c68c9f614f1e088f9c7267ea052d1193</originalsourceid><addsrcrecordid>eNp9kFtLwzAUgIMobl6efJc8iSB1ubVpEIQxvMFUmPoc0jSZ0a6pSSvs31vZHPri03k4H985fAAcYXSOkaCjWoXR_F0pxtItMMQ0IwkTGdkGQ0RRmmDE8gHYi_ENIcxwynbBgBKWUZaSIbi4V03j6jks_UK5OkJv4Xj2RKAOrnVaVdD6AF0b4exhDEuj1RJq1Sjt2uUB2LGqiuZwPffBy_XV8-Q2mT7e3E3G00QzTNqEUaJZluuC2CLDZWZZSTinlnCT84KTXPdLYTPMLDYoz63QnGTcKJSSEmNB98Hlytt0xcKU2tRtUJVsgluosJReOfl3U7tXOfefklPKBaW94HQtCP6jM7GVCxe1qSpVG99FSRjiKReCpD16tkJ18DEGYzdnMJLfuWWfW65z9_Tx78827E_fHjhZAb5r_jV9AXt9iEg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2407579925</pqid></control><display><type>article</type><title>Mapping domains of ARS2 critical for its RNA decay capacity</title><source>Oxford Journals Open Access Collection</source><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Melko, Mireille ; Winczura, Kinga ; Rouvière, Jérôme Olivier ; Oborská-Oplová, Michaela ; Andersen, Pia K ; Heick Jensen, Torben</creator><creatorcontrib>Melko, Mireille ; Winczura, Kinga ; Rouvière, Jérôme Olivier ; Oborská-Oplová, Michaela ; Andersen, Pia K ; Heick Jensen, Torben</creatorcontrib><description>Abstract
ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a degradation phenotype aided by its interaction with the poly(A) tail exosome targeting (PAXT) connection. Interestingly, C-terminal amino acids of ARS2, responsible for binding the RNA 5′cap binding complex (CBC), become dispensable when ARS2 is directly tethered to the reporter RNA. In contrast, the Zinc-finger (ZnF) domain of ARS2 is essential for the decay of both reporters and consistently co-immunoprecipitation analyses reveal a necessity of this domain for the interaction of ARS2 with the PAXT-associated RNA helicase MTR4. Taken together, our results map the domains of ARS2 underlying two essential properties of the protein: its RNP targeting ability and its capacity to recruit the RNA decay machinery.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkaa445</identifier><identifier>PMID: 32463452</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Exosome Multienzyme Ribonuclease Complex - genetics ; HEK293 Cells ; Humans ; Nuclear Cap-Binding Protein Complex - genetics ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Protein Domains - genetics ; RNA and RNA-protein complexes ; RNA Helicases - chemistry ; RNA Helicases - genetics ; RNA Stability - genetics ; RNA, Messenger - chemistry ; RNA, Messenger - genetics ; RNA, Nuclear - chemistry ; RNA, Nuclear - genetics</subject><ispartof>Nucleic acids research, 2020-07, Vol.48 (12), p.6943-6953</ispartof><rights>The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. 2020</rights><rights>The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-432c468cb2fb61d6f4d2773f27e87b728c68c9f614f1e088f9c7267ea052d1193</citedby><cites>FETCH-LOGICAL-c412t-432c468cb2fb61d6f4d2773f27e87b728c68c9f614f1e088f9c7267ea052d1193</cites><orcidid>0000-0001-5127-1239 ; 0000-0003-0976-4341</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/PMC7337933/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7337933/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,1598,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32463452$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Melko, Mireille</creatorcontrib><creatorcontrib>Winczura, Kinga</creatorcontrib><creatorcontrib>Rouvière, Jérôme Olivier</creatorcontrib><creatorcontrib>Oborská-Oplová, Michaela</creatorcontrib><creatorcontrib>Andersen, Pia K</creatorcontrib><creatorcontrib>Heick Jensen, Torben</creatorcontrib><title>Mapping domains of ARS2 critical for its RNA decay capacity</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Abstract
ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a degradation phenotype aided by its interaction with the poly(A) tail exosome targeting (PAXT) connection. Interestingly, C-terminal amino acids of ARS2, responsible for binding the RNA 5′cap binding complex (CBC), become dispensable when ARS2 is directly tethered to the reporter RNA. In contrast, the Zinc-finger (ZnF) domain of ARS2 is essential for the decay of both reporters and consistently co-immunoprecipitation analyses reveal a necessity of this domain for the interaction of ARS2 with the PAXT-associated RNA helicase MTR4. Taken together, our results map the domains of ARS2 underlying two essential properties of the protein: its RNP targeting ability and its capacity to recruit the RNA decay machinery.</description><subject>Exosome Multienzyme Ribonuclease Complex - genetics</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Nuclear Cap-Binding Protein Complex - genetics</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - genetics</subject><subject>Protein Domains - genetics</subject><subject>RNA and RNA-protein complexes</subject><subject>RNA Helicases - chemistry</subject><subject>RNA Helicases - genetics</subject><subject>RNA Stability - genetics</subject><subject>RNA, Messenger - chemistry</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Nuclear - chemistry</subject><subject>RNA, Nuclear - genetics</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>TOX</sourceid><sourceid>EIF</sourceid><recordid>eNp9kFtLwzAUgIMobl6efJc8iSB1ubVpEIQxvMFUmPoc0jSZ0a6pSSvs31vZHPri03k4H985fAAcYXSOkaCjWoXR_F0pxtItMMQ0IwkTGdkGQ0RRmmDE8gHYi_ENIcxwynbBgBKWUZaSIbi4V03j6jks_UK5OkJv4Xj2RKAOrnVaVdD6AF0b4exhDEuj1RJq1Sjt2uUB2LGqiuZwPffBy_XV8-Q2mT7e3E3G00QzTNqEUaJZluuC2CLDZWZZSTinlnCT84KTXPdLYTPMLDYoz63QnGTcKJSSEmNB98Hlytt0xcKU2tRtUJVsgluosJReOfl3U7tXOfefklPKBaW94HQtCP6jM7GVCxe1qSpVG99FSRjiKReCpD16tkJ18DEGYzdnMJLfuWWfW65z9_Tx78827E_fHjhZAb5r_jV9AXt9iEg</recordid><startdate>20200709</startdate><enddate>20200709</enddate><creator>Melko, Mireille</creator><creator>Winczura, Kinga</creator><creator>Rouvière, Jérôme Olivier</creator><creator>Oborská-Oplová, Michaela</creator><creator>Andersen, Pia K</creator><creator>Heick Jensen, Torben</creator><general>Oxford University Press</general><scope>TOX</scope><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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5127-1239</orcidid><orcidid>https://orcid.org/0000-0003-0976-4341</orcidid></search><sort><creationdate>20200709</creationdate><title>Mapping domains of ARS2 critical for its RNA decay capacity</title><author>Melko, Mireille ; Winczura, Kinga ; Rouvière, Jérôme Olivier ; Oborská-Oplová, Michaela ; Andersen, Pia K ; Heick Jensen, Torben</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-432c468cb2fb61d6f4d2773f27e87b728c68c9f614f1e088f9c7267ea052d1193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Exosome Multienzyme Ribonuclease Complex - genetics</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Nuclear Cap-Binding Protein Complex - genetics</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - genetics</topic><topic>Protein Domains - genetics</topic><topic>RNA and RNA-protein complexes</topic><topic>RNA Helicases - chemistry</topic><topic>RNA Helicases - genetics</topic><topic>RNA Stability - genetics</topic><topic>RNA, Messenger - chemistry</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Nuclear - chemistry</topic><topic>RNA, Nuclear - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Melko, Mireille</creatorcontrib><creatorcontrib>Winczura, Kinga</creatorcontrib><creatorcontrib>Rouvière, Jérôme Olivier</creatorcontrib><creatorcontrib>Oborská-Oplová, Michaela</creatorcontrib><creatorcontrib>Andersen, Pia K</creatorcontrib><creatorcontrib>Heick Jensen, Torben</creatorcontrib><collection>Oxford Journals Open Access Collection</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Melko, Mireille</au><au>Winczura, Kinga</au><au>Rouvière, Jérôme Olivier</au><au>Oborská-Oplová, Michaela</au><au>Andersen, Pia K</au><au>Heick Jensen, Torben</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mapping domains of ARS2 critical for its RNA decay capacity</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2020-07-09</date><risdate>2020</risdate><volume>48</volume><issue>12</issue><spage>6943</spage><epage>6953</epage><pages>6943-6953</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Abstract
ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a degradation phenotype aided by its interaction with the poly(A) tail exosome targeting (PAXT) connection. Interestingly, C-terminal amino acids of ARS2, responsible for binding the RNA 5′cap binding complex (CBC), become dispensable when ARS2 is directly tethered to the reporter RNA. In contrast, the Zinc-finger (ZnF) domain of ARS2 is essential for the decay of both reporters and consistently co-immunoprecipitation analyses reveal a necessity of this domain for the interaction of ARS2 with the PAXT-associated RNA helicase MTR4. Taken together, our results map the domains of ARS2 underlying two essential properties of the protein: its RNP targeting ability and its capacity to recruit the RNA decay machinery.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>32463452</pmid><doi>10.1093/nar/gkaa445</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-5127-1239</orcidid><orcidid>https://orcid.org/0000-0003-0976-4341</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0305-1048 |
ispartof | Nucleic acids research, 2020-07, Vol.48 (12), p.6943-6953 |
issn | 0305-1048 1362-4962 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7337933 |
source | Oxford Journals Open Access Collection; MEDLINE; DOAJ Directory of Open Access Journals; PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Exosome Multienzyme Ribonuclease Complex - genetics HEK293 Cells Humans Nuclear Cap-Binding Protein Complex - genetics Nuclear Proteins - chemistry Nuclear Proteins - genetics Protein Domains - genetics RNA and RNA-protein complexes RNA Helicases - chemistry RNA Helicases - genetics RNA Stability - genetics RNA, Messenger - chemistry RNA, Messenger - genetics RNA, Nuclear - chemistry RNA, Nuclear - genetics |
title | Mapping domains of ARS2 critical for its RNA decay capacity |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T00%3A17%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Mapping%20domains%20of%20ARS2%20critical%20for%20its%20RNA%20decay%20capacity&rft.jtitle=Nucleic%20acids%20research&rft.au=Melko,%20Mireille&rft.date=2020-07-09&rft.volume=48&rft.issue=12&rft.spage=6943&rft.epage=6953&rft.pages=6943-6953&rft.issn=0305-1048&rft.eissn=1362-4962&rft_id=info:doi/10.1093/nar/gkaa445&rft_dat=%3Cproquest_pubme%3E2407579925%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2407579925&rft_id=info:pmid/32463452&rft_oup_id=10.1093/nar/gkaa445&rfr_iscdi=true |