Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system
RNase LS was originally identified as a potential antagonist of bacteriophage T4 infection. When T4 dmd is defective, RNase LS activity rapidly increases after T4 infection and cleaves T4 mRNAs to antagonize T4 reproduction. Here we show that rnlA, a structural gene of RNase LS, encodes a novel toxi...
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| Veröffentlicht in: | Genetics (Austin) 2011-01, Vol.187 (1), p.123-130 |
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| creator | Koga, Mitsunori Otsuka, Yuichi Lemire, Sébastien Yonesaki, Tetsuro |
| description | RNase LS was originally identified as a potential antagonist of bacteriophage T4 infection. When T4 dmd is defective, RNase LS activity rapidly increases after T4 infection and cleaves T4 mRNAs to antagonize T4 reproduction. Here we show that rnlA, a structural gene of RNase LS, encodes a novel toxin, and that rnlB (formally yfjO), located immediately downstream of rnlA, encodes an antitoxin against RnlA. Ectopic expression of RnlA caused inhibition of cell growth and rapid degradation of mRNAs in ΔrnlAB cells. On the other hand, RnlB neutralized these RnlA effects. Furthermore, overexpression of RnlB in wild-type cells could completely suppress the growth defect of a T4 dmd mutant, that is, excess RnlB inhibited RNase LS activity. Pull-down analysis showed a specific interaction between RnlA and RnlB. Compared to RnlA, RnlB was extremely unstable, being degraded by ClpXP and Lon proteases, and this instability may increase RNase LS activity after T4 infection. All of these results suggested that rnlA-rnlB define a new toxin-antitoxin (TA) system. |
| doi_str_mv | 10.1534/genetics.110.121798 |
| format | Article |
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When T4 dmd is defective, RNase LS activity rapidly increases after T4 infection and cleaves T4 mRNAs to antagonize T4 reproduction. Here we show that rnlA, a structural gene of RNase LS, encodes a novel toxin, and that rnlB (formally yfjO), located immediately downstream of rnlA, encodes an antitoxin against RnlA. Ectopic expression of RnlA caused inhibition of cell growth and rapid degradation of mRNAs in ΔrnlAB cells. On the other hand, RnlB neutralized these RnlA effects. Furthermore, overexpression of RnlB in wild-type cells could completely suppress the growth defect of a T4 dmd mutant, that is, excess RnlB inhibited RNase LS activity. Pull-down analysis showed a specific interaction between RnlA and RnlB. Compared to RnlA, RnlB was extremely unstable, being degraded by ClpXP and Lon proteases, and this instability may increase RNase LS activity after T4 infection. All of these results suggested that rnlA-rnlB define a new toxin-antitoxin (TA) system.</description><identifier>ISSN: 1943-2631</identifier><identifier>ISSN: 0016-6731</identifier><identifier>EISSN: 1943-2631</identifier><identifier>DOI: 10.1534/genetics.110.121798</identifier><identifier>PMID: 20980243</identifier><identifier>CODEN: GENTAE</identifier><language>eng</language><publisher>United States: Genetics Society of America</publisher><subject>Antitoxins - chemistry ; Antitoxins - genetics ; Antitoxins - immunology ; Antitoxins - metabolism ; Bacteria ; Bacterial Toxins - chemistry ; Bacterial Toxins - immunology ; Bacterial Toxins - metabolism ; Bacteriology ; E coli ; Escherichia coli K12 - cytology ; Escherichia coli K12 - genetics ; Escherichia coli K12 - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - immunology ; Escherichia coli Proteins - metabolism ; Gene Expression Regulation, Bacterial ; Investigations ; Microbiology ; Mutation ; Operon - genetics ; Plasmids ; Protein Stability ; Ribonucleases - metabolism ; RNA Stability ; RNA, Messenger - chemistry ; RNA, Messenger - metabolism</subject><ispartof>Genetics (Austin), 2011-01, Vol.187 (1), p.123-130</ispartof><rights>Copyright Genetics Society of America Jan 2011</rights><rights>Copyright © 2011 by the Genetics Society of America 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-41589a3cf0875a71dc353f891eaec84fb6291effc27ca498ecffabdb39714ce53</citedby><cites>FETCH-LOGICAL-c497t-41589a3cf0875a71dc353f891eaec84fb6291effc27ca498ecffabdb39714ce53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20980243$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koga, Mitsunori</creatorcontrib><creatorcontrib>Otsuka, Yuichi</creatorcontrib><creatorcontrib>Lemire, Sébastien</creatorcontrib><creatorcontrib>Yonesaki, Tetsuro</creatorcontrib><title>Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system</title><title>Genetics (Austin)</title><addtitle>Genetics</addtitle><description>RNase LS was originally identified as a potential antagonist of bacteriophage T4 infection. When T4 dmd is defective, RNase LS activity rapidly increases after T4 infection and cleaves T4 mRNAs to antagonize T4 reproduction. Here we show that rnlA, a structural gene of RNase LS, encodes a novel toxin, and that rnlB (formally yfjO), located immediately downstream of rnlA, encodes an antitoxin against RnlA. Ectopic expression of RnlA caused inhibition of cell growth and rapid degradation of mRNAs in ΔrnlAB cells. On the other hand, RnlB neutralized these RnlA effects. Furthermore, overexpression of RnlB in wild-type cells could completely suppress the growth defect of a T4 dmd mutant, that is, excess RnlB inhibited RNase LS activity. Pull-down analysis showed a specific interaction between RnlA and RnlB. Compared to RnlA, RnlB was extremely unstable, being degraded by ClpXP and Lon proteases, and this instability may increase RNase LS activity after T4 infection. All of these results suggested that rnlA-rnlB define a new toxin-antitoxin (TA) system.</description><subject>Antitoxins - chemistry</subject><subject>Antitoxins - genetics</subject><subject>Antitoxins - immunology</subject><subject>Antitoxins - metabolism</subject><subject>Bacteria</subject><subject>Bacterial Toxins - chemistry</subject><subject>Bacterial Toxins - immunology</subject><subject>Bacterial Toxins - metabolism</subject><subject>Bacteriology</subject><subject>E coli</subject><subject>Escherichia coli K12 - cytology</subject><subject>Escherichia coli K12 - genetics</subject><subject>Escherichia coli K12 - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - immunology</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Investigations</subject><subject>Microbiology</subject><subject>Mutation</subject><subject>Operon - genetics</subject><subject>Plasmids</subject><subject>Protein Stability</subject><subject>Ribonucleases - metabolism</subject><subject>RNA Stability</subject><subject>RNA, Messenger - chemistry</subject><subject>RNA, Messenger - metabolism</subject><issn>1943-2631</issn><issn>0016-6731</issn><issn>1943-2631</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdUV1LwzAUDaL4Uf0FghRffKomTdomL4LK_ICBL_ocsuxmy2iTmbTD_Xtb3YYKgRxOzj333hyEzgm-JgVlNzNw0Fodr8nA5KQSfA8dE8FolpeU7P_CR-gkxgXGuBQFP0RHORYc54weo9Eo6jkEq-dWpdrXNg2uvkuVmw7gvqeapY-QqtT5FdRp6z-ty5Rr7TdK4zq20JyiA6PqCGebO0Hvj6O3h-ds_Pr08nA3zjQTVZsxUnChqDaYV4WqyFTTghouCCjQnJlJmffYGJ1XWjHBQRujJtMJFRVhGgqaoNsf32U3aWCqwbVB1XIZbKPCWnpl5d8XZ-dy5leSYsJpfxJ0tTEI_qOD2MrGRg11rRz4Lkret8IloVWvvPynXPguuH47yRknrCj7_0sQ_RHp4GMMYHajECyHkOQ2JEkG5jukvuri9xa7mm0q9AtHxJE9</recordid><startdate>201101</startdate><enddate>201101</enddate><creator>Koga, Mitsunori</creator><creator>Otsuka, Yuichi</creator><creator>Lemire, Sébastien</creator><creator>Yonesaki, Tetsuro</creator><general>Genetics Society of America</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>3V.</scope><scope>4T-</scope><scope>4U-</scope><scope>7QP</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201101</creationdate><title>Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system</title><author>Koga, Mitsunori ; Otsuka, Yuichi ; Lemire, Sébastien ; Yonesaki, Tetsuro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-41589a3cf0875a71dc353f891eaec84fb6291effc27ca498ecffabdb39714ce53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Antitoxins - 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metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koga, Mitsunori</creatorcontrib><creatorcontrib>Otsuka, Yuichi</creatorcontrib><creatorcontrib>Lemire, Sébastien</creatorcontrib><creatorcontrib>Yonesaki, Tetsuro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Docstoc</collection><collection>University Readers</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Genetics (Austin)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koga, Mitsunori</au><au>Otsuka, Yuichi</au><au>Lemire, Sébastien</au><au>Yonesaki, Tetsuro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system</atitle><jtitle>Genetics (Austin)</jtitle><addtitle>Genetics</addtitle><date>2011-01</date><risdate>2011</risdate><volume>187</volume><issue>1</issue><spage>123</spage><epage>130</epage><pages>123-130</pages><issn>1943-2631</issn><issn>0016-6731</issn><eissn>1943-2631</eissn><coden>GENTAE</coden><abstract>RNase LS was originally identified as a potential antagonist of bacteriophage T4 infection. When T4 dmd is defective, RNase LS activity rapidly increases after T4 infection and cleaves T4 mRNAs to antagonize T4 reproduction. Here we show that rnlA, a structural gene of RNase LS, encodes a novel toxin, and that rnlB (formally yfjO), located immediately downstream of rnlA, encodes an antitoxin against RnlA. Ectopic expression of RnlA caused inhibition of cell growth and rapid degradation of mRNAs in ΔrnlAB cells. On the other hand, RnlB neutralized these RnlA effects. Furthermore, overexpression of RnlB in wild-type cells could completely suppress the growth defect of a T4 dmd mutant, that is, excess RnlB inhibited RNase LS activity. Pull-down analysis showed a specific interaction between RnlA and RnlB. Compared to RnlA, RnlB was extremely unstable, being degraded by ClpXP and Lon proteases, and this instability may increase RNase LS activity after T4 infection. All of these results suggested that rnlA-rnlB define a new toxin-antitoxin (TA) system.</abstract><cop>United States</cop><pub>Genetics Society of America</pub><pmid>20980243</pmid><doi>10.1534/genetics.110.121798</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Genetics (Austin), 2011-01, Vol.187 (1), p.123-130 |
| issn | 1943-2631 0016-6731 1943-2631 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Antitoxins - chemistry Antitoxins - genetics Antitoxins - immunology Antitoxins - metabolism Bacteria Bacterial Toxins - chemistry Bacterial Toxins - immunology Bacterial Toxins - metabolism Bacteriology E coli Escherichia coli K12 - cytology Escherichia coli K12 - genetics Escherichia coli K12 - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - immunology Escherichia coli Proteins - metabolism Gene Expression Regulation, Bacterial Investigations Microbiology Mutation Operon - genetics Plasmids Protein Stability Ribonucleases - metabolism RNA Stability RNA, Messenger - chemistry RNA, Messenger - metabolism |
| title | Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system |
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