MicA sRNA links the PhoP regulon to cell envelope stress
Numerous small RNAs regulators of gene expression exist in bacteria. A large class of them binds to the RNA chaperone Hfq and act by base pairing interactions with their target mRNA, thereby affecting their translation and/or stability. They often have multiple direct targets, some of which may be r...
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| Veröffentlicht in: | Molecular microbiology 2010-04, Vol.76 (2), p.467-479 |
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| creator | Coornaert, Audrey Lu, Alisa Mandin, Pierre Springer, Mathias Gottesman, Susan Guillier, Maude |
| description | Numerous small RNAs regulators of gene expression exist in bacteria. A large class of them binds to the RNA chaperone Hfq and act by base pairing interactions with their target mRNA, thereby affecting their translation and/or stability. They often have multiple direct targets, some of which may be regulators themselves, and production of a single sRNA can therefore affect the expression of dozens of genes. We show in this study that the synthesis of the Escherichia coli pleiotropic PhoPQ two-component system is repressed by MicA, a σE-dependent sRNA regulator of porin biogenesis. MicA directly pairs with phoPQ mRNA in the translation initiation region of phoP and presumably inhibits translation by competing with ribosome binding. Consequently, MicA downregulates several members of the PhoPQ regulon. By linking PhoPQ to σE, our findings suggest that major cellular processes such as Mg²⁺ transport, virulence, LPS modification or resistance to antimicrobial peptides are modulated in response to envelope stress. In addition, we found that Hfq strongly affects the expression of phoP independently of MicA, raising the possibility that even more sRNAs, which remain to be identified, could regulate PhoPQ synthesis. |
| doi_str_mv | 10.1111/j.1365-2958.2010.07115.x |
| format | Article |
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A large class of them binds to the RNA chaperone Hfq and act by base pairing interactions with their target mRNA, thereby affecting their translation and/or stability. They often have multiple direct targets, some of which may be regulators themselves, and production of a single sRNA can therefore affect the expression of dozens of genes. We show in this study that the synthesis of the Escherichia coli pleiotropic PhoPQ two-component system is repressed by MicA, a σE-dependent sRNA regulator of porin biogenesis. MicA directly pairs with phoPQ mRNA in the translation initiation region of phoP and presumably inhibits translation by competing with ribosome binding. Consequently, MicA downregulates several members of the PhoPQ regulon. By linking PhoPQ to σE, our findings suggest that major cellular processes such as Mg²⁺ transport, virulence, LPS modification or resistance to antimicrobial peptides are modulated in response to envelope stress. In addition, we found that Hfq strongly affects the expression of phoP independently of MicA, raising the possibility that even more sRNAs, which remain to be identified, could regulate PhoPQ synthesis.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2010.07115.x</identifier><identifier>PMID: 20345657</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins - antagonists & inhibitors ; Bacterial Proteins - biosynthesis ; Biochemistry, Molecular Biology ; Biological and medical sciences ; Cell Membrane - metabolism ; Cell Wall - metabolism ; Cells ; E coli ; Escherichia coli - physiology ; Escherichia coli Proteins - antagonists & inhibitors ; Escherichia coli Proteins - biosynthesis ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation, Bacterial ; Genes ; Life Sciences ; Microbiology ; MicroRNAs - metabolism ; Mitochondria ; Protein Biosynthesis ; Regulon ; Ribonucleic acid ; RNA ; RNA, Messenger - metabolism ; Stress, Physiological</subject><ispartof>Molecular microbiology, 2010-04, Vol.76 (2), p.467-479</ispartof><rights>2010 Blackwell Publishing Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Ltd. 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A large class of them binds to the RNA chaperone Hfq and act by base pairing interactions with their target mRNA, thereby affecting their translation and/or stability. They often have multiple direct targets, some of which may be regulators themselves, and production of a single sRNA can therefore affect the expression of dozens of genes. We show in this study that the synthesis of the Escherichia coli pleiotropic PhoPQ two-component system is repressed by MicA, a σE-dependent sRNA regulator of porin biogenesis. MicA directly pairs with phoPQ mRNA in the translation initiation region of phoP and presumably inhibits translation by competing with ribosome binding. Consequently, MicA downregulates several members of the PhoPQ regulon. By linking PhoPQ to σE, our findings suggest that major cellular processes such as Mg²⁺ transport, virulence, LPS modification or resistance to antimicrobial peptides are modulated in response to envelope stress. In addition, we found that Hfq strongly affects the expression of phoP independently of MicA, raising the possibility that even more sRNAs, which remain to be identified, could regulate PhoPQ synthesis.</description><subject>Bacterial Proteins - antagonists & inhibitors</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Wall - metabolism</subject><subject>Cells</subject><subject>E coli</subject><subject>Escherichia coli - physiology</subject><subject>Escherichia coli Proteins - antagonists & inhibitors</subject><subject>Escherichia coli Proteins - biosynthesis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genes</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>MicroRNAs - metabolism</subject><subject>Mitochondria</subject><subject>Protein Biosynthesis</subject><subject>Regulon</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA, Messenger - metabolism</subject><subject>Stress, Physiological</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkl1v0zAYhS0EYmXwF8BCQoiLFH_EXxdDqiZgk1qYgEncWY7rtClpXOykbP8em5QCu8I3tl4_5z22jwGAGE1xGq83U0w5K4hickpQqiKBMZve3AOT48Z9MEGKoYJK8vUEPIpxgxCmiNOH4IQgWjLOxATIRWNnMH76MINt032LsF87eLX2VzC41dD6DvYeWte20HV71_qdg7EPLsbH4EFt2uieHOZTcP3u7Zfzi2L-8f3l-WxeWCYlK5a85FWNnKFUOKVExUomJJclstQoRaQwnHJqSYkrLowwpXO0klhao9ByaekpeDP23Q3V1i2t6_pgWr0LzdaEW-1No__d6Zq1Xvm9JoowQnFq8GpssL4ju5jNda4hxDDhVOwz-_JgFvz3wcVeb5uYb28654eoBaWYYyRpIp_fITd-CF16CY0VT8ZU8gTJEbLBxxhcffTHSOcg9UbnvHTOS-cg9a8g9U2SPv372kfh7-QS8OIAmGhNWwfT2Sb-4YhghFGVuLOR-9G07va_D6AXi8u8Svpno742XptVSB7Xn0n-SVgmj3SSn2Vuv4A</recordid><startdate>201004</startdate><enddate>201004</enddate><creator>Coornaert, Audrey</creator><creator>Lu, Alisa</creator><creator>Mandin, Pierre</creator><creator>Springer, Mathias</creator><creator>Gottesman, Susan</creator><creator>Guillier, Maude</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Wiley</general><scope>FBQ</scope><scope>IQODW</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>1XC</scope><scope>5PM</scope></search><sort><creationdate>201004</creationdate><title>MicA sRNA links the PhoP regulon to cell envelope stress</title><author>Coornaert, Audrey ; Lu, Alisa ; Mandin, Pierre ; Springer, Mathias ; Gottesman, Susan ; Guillier, Maude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5885-d646bf0ea337e997b545786840c3a99287a6363c241b67a7a4ee3b818ca90ddc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Bacterial Proteins - antagonists & inhibitors</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Wall - metabolism</topic><topic>Cells</topic><topic>E coli</topic><topic>Escherichia coli - physiology</topic><topic>Escherichia coli Proteins - antagonists & inhibitors</topic><topic>Escherichia coli Proteins - biosynthesis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Genes</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>MicroRNAs - metabolism</topic><topic>Mitochondria</topic><topic>Protein Biosynthesis</topic><topic>Regulon</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA, Messenger - metabolism</topic><topic>Stress, Physiological</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coornaert, Audrey</creatorcontrib><creatorcontrib>Lu, Alisa</creatorcontrib><creatorcontrib>Mandin, Pierre</creatorcontrib><creatorcontrib>Springer, Mathias</creatorcontrib><creatorcontrib>Gottesman, Susan</creatorcontrib><creatorcontrib>Guillier, Maude</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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 & 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>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coornaert, Audrey</au><au>Lu, Alisa</au><au>Mandin, Pierre</au><au>Springer, Mathias</au><au>Gottesman, Susan</au><au>Guillier, Maude</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MicA sRNA links the PhoP regulon to cell envelope stress</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2010-04</date><risdate>2010</risdate><volume>76</volume><issue>2</issue><spage>467</spage><epage>479</epage><pages>467-479</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Numerous small RNAs regulators of gene expression exist in bacteria. A large class of them binds to the RNA chaperone Hfq and act by base pairing interactions with their target mRNA, thereby affecting their translation and/or stability. They often have multiple direct targets, some of which may be regulators themselves, and production of a single sRNA can therefore affect the expression of dozens of genes. We show in this study that the synthesis of the Escherichia coli pleiotropic PhoPQ two-component system is repressed by MicA, a σE-dependent sRNA regulator of porin biogenesis. MicA directly pairs with phoPQ mRNA in the translation initiation region of phoP and presumably inhibits translation by competing with ribosome binding. Consequently, MicA downregulates several members of the PhoPQ regulon. By linking PhoPQ to σE, our findings suggest that major cellular processes such as Mg²⁺ transport, virulence, LPS modification or resistance to antimicrobial peptides are modulated in response to envelope stress. 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| ispartof | Molecular microbiology, 2010-04, Vol.76 (2), p.467-479 |
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| subjects | Bacterial Proteins - antagonists & inhibitors Bacterial Proteins - biosynthesis Biochemistry, Molecular Biology Biological and medical sciences Cell Membrane - metabolism Cell Wall - metabolism Cells E coli Escherichia coli - physiology Escherichia coli Proteins - antagonists & inhibitors Escherichia coli Proteins - biosynthesis Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation, Bacterial Genes Life Sciences Microbiology MicroRNAs - metabolism Mitochondria Protein Biosynthesis Regulon Ribonucleic acid RNA RNA, Messenger - metabolism Stress, Physiological |
| title | MicA sRNA links the PhoP regulon to cell envelope stress |
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