RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae

The cellular response to stress conditions involves a decision between survival or cell death when damage is severe. A conserved stress response in eukaryotes involves endonucleolytic cleavage of transfer RNAs (tRNAs). The mechanism and significance of such tRNA cleavage is unknown. We show that in...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of cell biology 2009-04, Vol.185 (1), p.43-50
Hauptverfasser: Thompson, Debrah M, Parker, Roy
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 50
container_issue 1
container_start_page 43
container_title The Journal of cell biology
container_volume 185
creator Thompson, Debrah M
Parker, Roy
description The cellular response to stress conditions involves a decision between survival or cell death when damage is severe. A conserved stress response in eukaryotes involves endonucleolytic cleavage of transfer RNAs (tRNAs). The mechanism and significance of such tRNA cleavage is unknown. We show that in yeast, tRNAs are cleaved by the RNase T2 family member Rny1p, which is released from the vacuole into the cytosol during oxidative stress. Rny1p modulates yeast cell survival during oxidative stress independently of its catalytic ability. This suggests that upon release to the cytosol, Rny1p promotes cell death by direct interactions with downstream components. Thus, detection of Rny1p, and possibly its orthologues, in the cytosol may be a conserved mechanism for assessing cellular damage and determining cell survival, analogous to the role of cytochrome c as a marker for mitochondrial damage.
doi_str_mv 10.1083/jcb.200811119
format Article
fullrecord <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2700514</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>20537227</jstor_id><sourcerecordid>20537227</sourcerecordid><originalsourceid>FETCH-LOGICAL-c524t-7133ee7e6d3e4b48c243d116264d4f58b0e7a22f244f818fd2c99f03a51b141e3</originalsourceid><addsrcrecordid>eNpdkc2P0zAQxS0EYsvCkSNgceCWZcZ24uSCtFrxJa0WqcueLceZtK7auNhJRf97XFqVD19G8vvN0xs9xl4iXCHU8v3KtVcCoMb8mkdshqWCokYFj9kMQGDRlKK8YM9SWgGA0ko-ZRfYSCnqBmeM5nc2EZ8Pe9xytya7o8TH-d114nbo-DaGTRjzl6P1mndkxyXvpuiHBQ8_fWdHvyOexkgpcT_we-vc0uadvfu9E2nnk7f0nD3p7TrRi9O8ZA-fPn6_-VLcfvv89eb6tnClUGOhUUoiTVUnSbWqdkLJDrESlepUX9YtkLZC9EKpvsa674Rrmh6kLbFFhSQv2Yej73ZqN9Q5GsZo12Yb_cbGvQnWm3-VwS_NIuyM0AAlqmzw7mQQw4-J0mg2Ph1utwOFKZlKo2hqKDP49j9wFaY45OOMQI2gGt1kqDhCLoaUIvXnJAjm0J7J7Zlze5l__Xf8P_Sprgy8OgKrNIZ41kUOpIXQWX9z1HsbjF1En8zDvQCUgBXqA_YLapao9g</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217104979</pqid></control><display><type>article</type><title>RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>EZB Electronic Journals Library</source><creator>Thompson, Debrah M ; Parker, Roy</creator><creatorcontrib>Thompson, Debrah M ; Parker, Roy</creatorcontrib><description>The cellular response to stress conditions involves a decision between survival or cell death when damage is severe. A conserved stress response in eukaryotes involves endonucleolytic cleavage of transfer RNAs (tRNAs). The mechanism and significance of such tRNA cleavage is unknown. We show that in yeast, tRNAs are cleaved by the RNase T2 family member Rny1p, which is released from the vacuole into the cytosol during oxidative stress. Rny1p modulates yeast cell survival during oxidative stress independently of its catalytic ability. This suggests that upon release to the cytosol, Rny1p promotes cell death by direct interactions with downstream components. Thus, detection of Rny1p, and possibly its orthologues, in the cytosol may be a conserved mechanism for assessing cellular damage and determining cell survival, analogous to the role of cytochrome c as a marker for mitochondrial damage.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200811119</identifier><identifier>PMID: 19332891</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Apoptosis ; Apoptosis - physiology ; Biochemistry ; Cell death ; Cell lines ; Cytosol ; Cytosol - enzymology ; Cytosol - metabolism ; Eukaryotes ; Humans ; Oxidative Stress ; Protein synthesis ; Ribonucleases - genetics ; Ribonucleases - metabolism ; Ribonucleases - physiology ; RNA, Transfer - metabolism ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - physiology ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - physiology ; Steepest descent method ; Transfer RNA ; Tumor Suppressor Proteins - genetics ; Tumor Suppressor Proteins - metabolism ; Tumor Suppressor Proteins - physiology ; Tumors ; Vacuoles ; Vacuoles - enzymology ; Yeast ; Yeasts</subject><ispartof>The Journal of cell biology, 2009-04, Vol.185 (1), p.43-50</ispartof><rights>Copyright Rockefeller University Press Apr 6, 2009</rights><rights>2009 Thompson and Parker 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-7133ee7e6d3e4b48c243d116264d4f58b0e7a22f244f818fd2c99f03a51b141e3</citedby><cites>FETCH-LOGICAL-c524t-7133ee7e6d3e4b48c243d116264d4f58b0e7a22f244f818fd2c99f03a51b141e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19332891$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thompson, Debrah M</creatorcontrib><creatorcontrib>Parker, Roy</creatorcontrib><title>RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The cellular response to stress conditions involves a decision between survival or cell death when damage is severe. A conserved stress response in eukaryotes involves endonucleolytic cleavage of transfer RNAs (tRNAs). The mechanism and significance of such tRNA cleavage is unknown. We show that in yeast, tRNAs are cleaved by the RNase T2 family member Rny1p, which is released from the vacuole into the cytosol during oxidative stress. Rny1p modulates yeast cell survival during oxidative stress independently of its catalytic ability. This suggests that upon release to the cytosol, Rny1p promotes cell death by direct interactions with downstream components. Thus, detection of Rny1p, and possibly its orthologues, in the cytosol may be a conserved mechanism for assessing cellular damage and determining cell survival, analogous to the role of cytochrome c as a marker for mitochondrial damage.</description><subject>Apoptosis</subject><subject>Apoptosis - physiology</subject><subject>Biochemistry</subject><subject>Cell death</subject><subject>Cell lines</subject><subject>Cytosol</subject><subject>Cytosol - enzymology</subject><subject>Cytosol - metabolism</subject><subject>Eukaryotes</subject><subject>Humans</subject><subject>Oxidative Stress</subject><subject>Protein synthesis</subject><subject>Ribonucleases - genetics</subject><subject>Ribonucleases - metabolism</subject><subject>Ribonucleases - physiology</subject><subject>RNA, Transfer - metabolism</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>Steepest descent method</subject><subject>Transfer RNA</subject><subject>Tumor Suppressor Proteins - genetics</subject><subject>Tumor Suppressor Proteins - metabolism</subject><subject>Tumor Suppressor Proteins - physiology</subject><subject>Tumors</subject><subject>Vacuoles</subject><subject>Vacuoles - enzymology</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc2P0zAQxS0EYsvCkSNgceCWZcZ24uSCtFrxJa0WqcueLceZtK7auNhJRf97XFqVD19G8vvN0xs9xl4iXCHU8v3KtVcCoMb8mkdshqWCokYFj9kMQGDRlKK8YM9SWgGA0ko-ZRfYSCnqBmeM5nc2EZ8Pe9xytya7o8TH-d114nbo-DaGTRjzl6P1mndkxyXvpuiHBQ8_fWdHvyOexkgpcT_we-vc0uadvfu9E2nnk7f0nD3p7TrRi9O8ZA-fPn6_-VLcfvv89eb6tnClUGOhUUoiTVUnSbWqdkLJDrESlepUX9YtkLZC9EKpvsa674Rrmh6kLbFFhSQv2Yej73ZqN9Q5GsZo12Yb_cbGvQnWm3-VwS_NIuyM0AAlqmzw7mQQw4-J0mg2Ph1utwOFKZlKo2hqKDP49j9wFaY45OOMQI2gGt1kqDhCLoaUIvXnJAjm0J7J7Zlze5l__Xf8P_Sprgy8OgKrNIZ41kUOpIXQWX9z1HsbjF1En8zDvQCUgBXqA_YLapao9g</recordid><startdate>20090406</startdate><enddate>20090406</enddate><creator>Thompson, Debrah M</creator><creator>Parker, Roy</creator><general>The Rockefeller University Press</general><general>Rockefeller University Press</general><scope>FBQ</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090406</creationdate><title>RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae</title><author>Thompson, Debrah M ; Parker, Roy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c524t-7133ee7e6d3e4b48c243d116264d4f58b0e7a22f244f818fd2c99f03a51b141e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Apoptosis</topic><topic>Apoptosis - physiology</topic><topic>Biochemistry</topic><topic>Cell death</topic><topic>Cell lines</topic><topic>Cytosol</topic><topic>Cytosol - enzymology</topic><topic>Cytosol - metabolism</topic><topic>Eukaryotes</topic><topic>Humans</topic><topic>Oxidative Stress</topic><topic>Protein synthesis</topic><topic>Ribonucleases - genetics</topic><topic>Ribonucleases - metabolism</topic><topic>Ribonucleases - physiology</topic><topic>RNA, Transfer - metabolism</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>Steepest descent method</topic><topic>Transfer RNA</topic><topic>Tumor Suppressor Proteins - genetics</topic><topic>Tumor Suppressor Proteins - metabolism</topic><topic>Tumor Suppressor Proteins - physiology</topic><topic>Tumors</topic><topic>Vacuoles</topic><topic>Vacuoles - enzymology</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thompson, Debrah M</creatorcontrib><creatorcontrib>Parker, Roy</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thompson, Debrah M</au><au>Parker, Roy</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2009-04-06</date><risdate>2009</risdate><volume>185</volume><issue>1</issue><spage>43</spage><epage>50</epage><pages>43-50</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The cellular response to stress conditions involves a decision between survival or cell death when damage is severe. A conserved stress response in eukaryotes involves endonucleolytic cleavage of transfer RNAs (tRNAs). The mechanism and significance of such tRNA cleavage is unknown. We show that in yeast, tRNAs are cleaved by the RNase T2 family member Rny1p, which is released from the vacuole into the cytosol during oxidative stress. Rny1p modulates yeast cell survival during oxidative stress independently of its catalytic ability. This suggests that upon release to the cytosol, Rny1p promotes cell death by direct interactions with downstream components. Thus, detection of Rny1p, and possibly its orthologues, in the cytosol may be a conserved mechanism for assessing cellular damage and determining cell survival, analogous to the role of cytochrome c as a marker for mitochondrial damage.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>19332891</pmid><doi>10.1083/jcb.200811119</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9525
ispartof The Journal of cell biology, 2009-04, Vol.185 (1), p.43-50
issn 0021-9525
1540-8140
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2700514
source MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library
subjects Apoptosis
Apoptosis - physiology
Biochemistry
Cell death
Cell lines
Cytosol
Cytosol - enzymology
Cytosol - metabolism
Eukaryotes
Humans
Oxidative Stress
Protein synthesis
Ribonucleases - genetics
Ribonucleases - metabolism
Ribonucleases - physiology
RNA, Transfer - metabolism
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - physiology
Steepest descent method
Transfer RNA
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
Tumor Suppressor Proteins - physiology
Tumors
Vacuoles
Vacuoles - enzymology
Yeast
Yeasts
title RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-20T21%3A41%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=RNase%20Rny1p%20cleaves%20tRNAs%20and%20promotes%20cell%20death%20during%20oxidative%20stress%20in%20Saccharomyces%20cerevisiae&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Thompson,%20Debrah%20M&rft.date=2009-04-06&rft.volume=185&rft.issue=1&rft.spage=43&rft.epage=50&rft.pages=43-50&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.200811119&rft_dat=%3Cjstor_pubme%3E20537227%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217104979&rft_id=info:pmid/19332891&rft_jstor_id=20537227&rfr_iscdi=true