Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding
The adaptation of mRNA stability to environmental changes is a means of cells to adjust the level of gene expression. The Escherichia coli ompA mRNA has served as one of the paradigms for regulated mRNA decay in prokaryotes. The stability of the transcript is known to be correlated inversely with th...
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| Veröffentlicht in: | Genes & development 2000-05, Vol.14 (9), p.1109-1118 |
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| creator | Vytvytska, O Moll, I Kaberdin, V R von Gabain, A Bläsi, U |
| description | The adaptation of mRNA stability to environmental changes is a means of cells to adjust the level of gene expression. The Escherichia coli ompA mRNA has served as one of the paradigms for regulated mRNA decay in prokaryotes. The stability of the transcript is known to be correlated inversely with the bacterial growth rate. Thus, the regulation of ompA mRNA stability meets the physiological needs to adjust the level of ompA expression to the rate of cell division. Recently, host factor I (Hfq/HF1) was shown to be involved in the regulation of ompA mRNA stability under slow growth conditions. Here, we present the first direct demonstration that 30S ribosomes bound to the ompA 5'-UTR protect the transcript from RNase E cleavage in vitro. However, the 30S protection was found to be abrogated in the presence of Hfq. Toeprinting and in vitro translation assays revealed that translation of ompA is repressed in the presence of Hfq. These in vitro studies are corroborated by in vivo expression studies demonstrating that the reduced synthesis rate of OmpA effected by Hfq results in functional inactivation of the ompA mRNA. The data are discussed in terms of a model wherein Hfq regulates the stability of ompA mRNA by competing with 30S ribosomes for binding to the ompA 5'-UTR. |
| doi_str_mv | 10.1101/gad.14.9.1109 |
| format | Article |
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The Escherichia coli ompA mRNA has served as one of the paradigms for regulated mRNA decay in prokaryotes. The stability of the transcript is known to be correlated inversely with the bacterial growth rate. Thus, the regulation of ompA mRNA stability meets the physiological needs to adjust the level of ompA expression to the rate of cell division. Recently, host factor I (Hfq/HF1) was shown to be involved in the regulation of ompA mRNA stability under slow growth conditions. Here, we present the first direct demonstration that 30S ribosomes bound to the ompA 5'-UTR protect the transcript from RNase E cleavage in vitro. However, the 30S protection was found to be abrogated in the presence of Hfq. Toeprinting and in vitro translation assays revealed that translation of ompA is repressed in the presence of Hfq. These in vitro studies are corroborated by in vivo expression studies demonstrating that the reduced synthesis rate of OmpA effected by Hfq results in functional inactivation of the ompA mRNA. The data are discussed in terms of a model wherein Hfq regulates the stability of ompA mRNA by competing with 30S ribosomes for binding to the ompA 5'-UTR.</description><identifier>ISSN: 0890-9369</identifier><identifier>EISSN: 1549-5477</identifier><identifier>DOI: 10.1101/gad.14.9.1109</identifier><identifier>PMID: 10809669</identifier><language>eng</language><publisher>United States: Cold Spring Harbor Laboratory Press</publisher><subject>5' Untranslated Regions - genetics ; Bacterial Outer Membrane Proteins - genetics ; Base Sequence ; Binding Sites ; Carrier Proteins - metabolism ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - growth & development ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; Hfq protein ; Host Factor 1 Protein ; Integration Host Factors ; Molecular Sequence Data ; Nucleic Acid Conformation ; OmpA protein ; Protein Biosynthesis ; Research Paper ; Ribosomes - metabolism ; RNA, Bacterial - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA-Binding Proteins - metabolism</subject><ispartof>Genes & development, 2000-05, Vol.14 (9), p.1109-1118</ispartof><rights>Copyright © 2000, Cold Spring Harbor Laboratory Press 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-b1ae682dfa55b0d5c4f5e4bece7788125faa14fc90f57f569ae2d03f7b546ff43</citedby><cites>FETCH-LOGICAL-c413t-b1ae682dfa55b0d5c4f5e4bece7788125faa14fc90f57f569ae2d03f7b546ff43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC316587/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC316587/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27911,27912,53778,53780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10809669$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vytvytska, O</creatorcontrib><creatorcontrib>Moll, I</creatorcontrib><creatorcontrib>Kaberdin, V R</creatorcontrib><creatorcontrib>von Gabain, A</creatorcontrib><creatorcontrib>Bläsi, U</creatorcontrib><title>Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding</title><title>Genes & development</title><addtitle>Genes Dev</addtitle><description>The adaptation of mRNA stability to environmental changes is a means of cells to adjust the level of gene expression. The Escherichia coli ompA mRNA has served as one of the paradigms for regulated mRNA decay in prokaryotes. The stability of the transcript is known to be correlated inversely with the bacterial growth rate. Thus, the regulation of ompA mRNA stability meets the physiological needs to adjust the level of ompA expression to the rate of cell division. Recently, host factor I (Hfq/HF1) was shown to be involved in the regulation of ompA mRNA stability under slow growth conditions. Here, we present the first direct demonstration that 30S ribosomes bound to the ompA 5'-UTR protect the transcript from RNase E cleavage in vitro. However, the 30S protection was found to be abrogated in the presence of Hfq. Toeprinting and in vitro translation assays revealed that translation of ompA is repressed in the presence of Hfq. These in vitro studies are corroborated by in vivo expression studies demonstrating that the reduced synthesis rate of OmpA effected by Hfq results in functional inactivation of the ompA mRNA. The data are discussed in terms of a model wherein Hfq regulates the stability of ompA mRNA by competing with 30S ribosomes for binding to the ompA 5'-UTR.</description><subject>5' Untranslated Regions - genetics</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Carrier Proteins - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - growth & development</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Hfq protein</subject><subject>Host Factor 1 Protein</subject><subject>Integration Host Factors</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>OmpA protein</subject><subject>Protein Biosynthesis</subject><subject>Research Paper</subject><subject>Ribosomes - metabolism</subject><subject>RNA, Bacterial - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - metabolism</subject><issn>0890-9369</issn><issn>1549-5477</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctLAzEQxoMoWh9Hr5KT6GFrZjePzcFDEbVCURA9h-zupEb2UZOt0v_eLS2iJ0_DN_ObYWY-Qk6BjQEYXM1tNQY-1muld8gIBNeJ4ErtkhHLNUt0JvUBOYzxnTEmmZT75ABYzrSUekQepu6DXkzv4JLG3jfL2vYYadcsJrR5fpzQCku7osWK-rbH4DD4dk6_fP9Ggy-62DVIC99WQ_aY7DlbRzzZxiPyenf7cjNNZk_3DzeTWVJyyPqkAIsyTytnhShYJUruBPICS1QqzyEVzlrgrtTMCeWE1BbTimVOFYJL53h2RK43cxfLosGqxLYPtjaL4BsbVqaz3vyttP7NzLtPk4EUuRr6z7f9oftYYuxN42OJdW1b7JbRqOGRXKb_g6AEh1StwWQDlqGLMaD7WQaYWZtkBpMMcKPXSg_82e8LftEbV7JvtPCOUA</recordid><startdate>20000501</startdate><enddate>20000501</enddate><creator>Vytvytska, O</creator><creator>Moll, I</creator><creator>Kaberdin, V R</creator><creator>von Gabain, A</creator><creator>Bläsi, U</creator><general>Cold Spring Harbor Laboratory Press</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000501</creationdate><title>Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding</title><author>Vytvytska, O ; 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The Escherichia coli ompA mRNA has served as one of the paradigms for regulated mRNA decay in prokaryotes. The stability of the transcript is known to be correlated inversely with the bacterial growth rate. Thus, the regulation of ompA mRNA stability meets the physiological needs to adjust the level of ompA expression to the rate of cell division. Recently, host factor I (Hfq/HF1) was shown to be involved in the regulation of ompA mRNA stability under slow growth conditions. Here, we present the first direct demonstration that 30S ribosomes bound to the ompA 5'-UTR protect the transcript from RNase E cleavage in vitro. However, the 30S protection was found to be abrogated in the presence of Hfq. Toeprinting and in vitro translation assays revealed that translation of ompA is repressed in the presence of Hfq. 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| subjects | 5' Untranslated Regions - genetics Bacterial Outer Membrane Proteins - genetics Base Sequence Binding Sites Carrier Proteins - metabolism Escherichia coli Escherichia coli - genetics Escherichia coli - growth & development Escherichia coli - metabolism Escherichia coli Proteins Gene Expression Regulation, Bacterial Hfq protein Host Factor 1 Protein Integration Host Factors Molecular Sequence Data Nucleic Acid Conformation OmpA protein Protein Biosynthesis Research Paper Ribosomes - metabolism RNA, Bacterial - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism RNA-Binding Proteins - metabolism |
| title | Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding |
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