Mtr4 RNA helicase structures and interactions
Mtr4 is a Ski2-like RNA helicase that plays a central role in RNA surveillance and degradation pathways as an activator of the RNA exosome. Multiple crystallographic and cryo-EM studies over the past 10 years have revealed important insight into the Mtr4 structure and interactions with protein and n...
Gespeichert in:
Veröffentlicht in: | Biological chemistry 2021-04, Vol.402 (5), p.605-616 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 616 |
---|---|
container_issue | 5 |
container_start_page | 605 |
container_title | Biological chemistry |
container_volume | 402 |
creator | Olsen, Keith J. Johnson, Sean J. |
description | Mtr4 is a Ski2-like RNA helicase that plays a central role in RNA surveillance and degradation pathways as an activator of the RNA exosome. Multiple crystallographic and cryo-EM studies over the past 10 years have revealed important insight into the Mtr4 structure and interactions with protein and nucleic acid binding partners. These structures place Mtr4 at the center of a dynamic process that recruits RNA substrates and presents them to the exosome. In this review, we summarize the available Mtr4 structures and highlight gaps in our current understanding. |
doi_str_mv | 10.1515/hsz-2020-0329 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8247069</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2514598090</sourcerecordid><originalsourceid>FETCH-LOGICAL-c440t-c2ebfe23be2428d8bf17519fd32d1c3454cc583ac68ee36aaa8ab5d8e840c9f03</originalsourceid><addsrcrecordid>eNptkMtLxDAQh4Mo7vo4epUevUQnrzYFEZbFF_gA0XNI06lb6bZrkir619t1VRQ8zQ_m4zfDR8geg0OmmDqahXfKgQMFwfM1MmZSZFQKptY_M6NpJmBEtkJ4AgANUmySkRBaZSJlY0Kvo5fJ3c0kmWFTOxswCdH3LvYeQ2LbMqnbiN66WHdt2CEblW0C7n7NbfJwdno_vaBXt-eX08kVdVJCpI5jUSEXBXLJdamLimWK5VUpeMmckEo6p7SwLtWIIrXWaluoUqOW4PIKxDY5WfUu-mKOpcM2etuYha_n1r-Zztbm76atZ-axezGaywzSfCg4-Crw3XOPIZp5HRw2jW2x64PhikmVa8iXt-gKdb4LwWP1c4aBWSo2g2KzVGyWigd-__dvP_S30wE4XgGvthnUlfjo-7chmKeu9-2g7f9iCVyloMQH9oyL2w</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2514598090</pqid></control><display><type>article</type><title>Mtr4 RNA helicase structures and interactions</title><source>De Gruyter journals</source><creator>Olsen, Keith J. ; Johnson, Sean J.</creator><creatorcontrib>Olsen, Keith J. ; Johnson, Sean J.</creatorcontrib><description>Mtr4 is a Ski2-like RNA helicase that plays a central role in RNA surveillance and degradation pathways as an activator of the RNA exosome. Multiple crystallographic and cryo-EM studies over the past 10 years have revealed important insight into the Mtr4 structure and interactions with protein and nucleic acid binding partners. These structures place Mtr4 at the center of a dynamic process that recruits RNA substrates and presents them to the exosome. In this review, we summarize the available Mtr4 structures and highlight gaps in our current understanding.</description><identifier>ISSN: 1431-6730</identifier><identifier>EISSN: 1437-4315</identifier><identifier>DOI: 10.1515/hsz-2020-0329</identifier><identifier>PMID: 33857361</identifier><language>eng</language><publisher>Germany: De Gruyter</publisher><subject>Mtr4 ; RNA helicase ; RNA surveillance ; Ski2-like helicase ; structure</subject><ispartof>Biological chemistry, 2021-04, Vol.402 (5), p.605-616</ispartof><rights>2020 Walter de Gruyter GmbH, Berlin/Boston.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-c2ebfe23be2428d8bf17519fd32d1c3454cc583ac68ee36aaa8ab5d8e840c9f03</citedby><cites>FETCH-LOGICAL-c440t-c2ebfe23be2428d8bf17519fd32d1c3454cc583ac68ee36aaa8ab5d8e840c9f03</cites><orcidid>0000-0001-7992-2494</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.degruyter.com/document/doi/10.1515/hsz-2020-0329/pdf$$EPDF$$P50$$Gwalterdegruyter$$H</linktopdf><linktohtml>$$Uhttps://www.degruyter.com/document/doi/10.1515/hsz-2020-0329/html$$EHTML$$P50$$Gwalterdegruyter$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,66497,68281</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33857361$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Olsen, Keith J.</creatorcontrib><creatorcontrib>Johnson, Sean J.</creatorcontrib><title>Mtr4 RNA helicase structures and interactions</title><title>Biological chemistry</title><addtitle>Biol Chem</addtitle><description>Mtr4 is a Ski2-like RNA helicase that plays a central role in RNA surveillance and degradation pathways as an activator of the RNA exosome. Multiple crystallographic and cryo-EM studies over the past 10 years have revealed important insight into the Mtr4 structure and interactions with protein and nucleic acid binding partners. These structures place Mtr4 at the center of a dynamic process that recruits RNA substrates and presents them to the exosome. In this review, we summarize the available Mtr4 structures and highlight gaps in our current understanding.</description><subject>Mtr4</subject><subject>RNA helicase</subject><subject>RNA surveillance</subject><subject>Ski2-like helicase</subject><subject>structure</subject><issn>1431-6730</issn><issn>1437-4315</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNptkMtLxDAQh4Mo7vo4epUevUQnrzYFEZbFF_gA0XNI06lb6bZrkir619t1VRQ8zQ_m4zfDR8geg0OmmDqahXfKgQMFwfM1MmZSZFQKptY_M6NpJmBEtkJ4AgANUmySkRBaZSJlY0Kvo5fJ3c0kmWFTOxswCdH3LvYeQ2LbMqnbiN66WHdt2CEblW0C7n7NbfJwdno_vaBXt-eX08kVdVJCpI5jUSEXBXLJdamLimWK5VUpeMmckEo6p7SwLtWIIrXWaluoUqOW4PIKxDY5WfUu-mKOpcM2etuYha_n1r-Zztbm76atZ-axezGaywzSfCg4-Crw3XOPIZp5HRw2jW2x64PhikmVa8iXt-gKdb4LwWP1c4aBWSo2g2KzVGyWigd-__dvP_S30wE4XgGvthnUlfjo-7chmKeu9-2g7f9iCVyloMQH9oyL2w</recordid><startdate>20210427</startdate><enddate>20210427</enddate><creator>Olsen, Keith J.</creator><creator>Johnson, Sean J.</creator><general>De Gruyter</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-7992-2494</orcidid></search><sort><creationdate>20210427</creationdate><title>Mtr4 RNA helicase structures and interactions</title><author>Olsen, Keith J. ; Johnson, Sean J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-c2ebfe23be2428d8bf17519fd32d1c3454cc583ac68ee36aaa8ab5d8e840c9f03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Mtr4</topic><topic>RNA helicase</topic><topic>RNA surveillance</topic><topic>Ski2-like helicase</topic><topic>structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olsen, Keith J.</creatorcontrib><creatorcontrib>Johnson, Sean J.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Olsen, Keith J.</au><au>Johnson, Sean J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mtr4 RNA helicase structures and interactions</atitle><jtitle>Biological chemistry</jtitle><addtitle>Biol Chem</addtitle><date>2021-04-27</date><risdate>2021</risdate><volume>402</volume><issue>5</issue><spage>605</spage><epage>616</epage><pages>605-616</pages><issn>1431-6730</issn><eissn>1437-4315</eissn><abstract>Mtr4 is a Ski2-like RNA helicase that plays a central role in RNA surveillance and degradation pathways as an activator of the RNA exosome. Multiple crystallographic and cryo-EM studies over the past 10 years have revealed important insight into the Mtr4 structure and interactions with protein and nucleic acid binding partners. These structures place Mtr4 at the center of a dynamic process that recruits RNA substrates and presents them to the exosome. In this review, we summarize the available Mtr4 structures and highlight gaps in our current understanding.</abstract><cop>Germany</cop><pub>De Gruyter</pub><pmid>33857361</pmid><doi>10.1515/hsz-2020-0329</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-7992-2494</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1431-6730 |
ispartof | Biological chemistry, 2021-04, Vol.402 (5), p.605-616 |
issn | 1431-6730 1437-4315 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8247069 |
source | De Gruyter journals |
subjects | Mtr4 RNA helicase RNA surveillance Ski2-like helicase structure |
title | Mtr4 RNA helicase structures and interactions |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T13%3A00%3A19IST&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=Mtr4%20RNA%20helicase%20structures%20and%20interactions&rft.jtitle=Biological%20chemistry&rft.au=Olsen,%20Keith%20J.&rft.date=2021-04-27&rft.volume=402&rft.issue=5&rft.spage=605&rft.epage=616&rft.pages=605-616&rft.issn=1431-6730&rft.eissn=1437-4315&rft_id=info:doi/10.1515/hsz-2020-0329&rft_dat=%3Cproquest_pubme%3E2514598090%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=2514598090&rft_id=info:pmid/33857361&rfr_iscdi=true |