tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens
Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modi...
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description | Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modification is essential for translational efficiency. Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually with the tRNA. Approximately, 100 tRNA modification enzymes have been identified with glucose-inhibited division (GidA) protein and MnmE being two of the enzymes studied. In Escherichia coli and Salmonella, GidA and MnmE bind together to form a functional complex responsible for the proper biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm⁵s²U34) of tRNAs. Studies have implicated this pathway in a major pathogenic regulatory mechanism as deletion of gidA and/or mnmE has attenuated several bacterial pathogens like Salmonella enterica serovar Typhimurium, Pseudomonas syringae, Aeromonas hydrophila, and many others. In this review, we summarize the potential role of the GidA/MnmE tRNA modification pathway in bacterial virulence, interactions with the host, and potential therapeutic strategies resulting from a greater understanding of this regulatory mechanism. |
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These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modification is essential for translational efficiency. Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually with the tRNA. Approximately, 100 tRNA modification enzymes have been identified with glucose-inhibited division (GidA) protein and MnmE being two of the enzymes studied. In Escherichia coli and Salmonella, GidA and MnmE bind together to form a functional complex responsible for the proper biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm⁵s²U34) of tRNAs. Studies have implicated this pathway in a major pathogenic regulatory mechanism as deletion of gidA and/or mnmE has attenuated several bacterial pathogens like Salmonella enterica serovar Typhimurium, Pseudomonas syringae, Aeromonas hydrophila, and many others. In this review, we summarize the potential role of the GidA/MnmE tRNA modification pathway in bacterial virulence, interactions with the host, and potential therapeutic strategies resulting from a greater understanding of this regulatory mechanism.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms151018267</identifier><identifier>PMID: 25310651</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Aeromonas hydrophila ; Animals ; Bacteria - pathogenicity ; Bacterial infections ; Bacterial Infections - metabolism ; Bacterial Infections - pathology ; Bacterial Physiological Phenomena ; Bacterial Proteins - metabolism ; Enzymes ; Escherichia coli ; Escherichia coli - pathogenicity ; Escherichia coli - physiology ; Escherichia coli Proteins - metabolism ; GTP Phosphohydrolases - metabolism ; Host-Pathogen Interactions ; Humans ; Pathogenesis ; Pseudomonas syringae ; Review ; RNA, Transfer - metabolism ; Salmonella enterica ; Transfer RNA ; Virulence ; Virulence Factors - metabolism</subject><ispartof>International journal of molecular sciences, 2014-10, Vol.15 (10), p.18267-18280</ispartof><rights>Copyright MDPI AG 2014</rights><rights>2014 by the authors; licensee MDPI, Basel, Switzerland. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c448t-df16ad8efd538b7d8ae9481f8facb969679fbbed4bcf1ba702d14d615736b3523</citedby><cites>FETCH-LOGICAL-c448t-df16ad8efd538b7d8ae9481f8facb969679fbbed4bcf1ba702d14d615736b3523</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/PMC4227215/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4227215/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25310651$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shippy, Daniel C</creatorcontrib><creatorcontrib>Fadl, Amin A</creatorcontrib><title>tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modification is essential for translational efficiency. Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually with the tRNA. Approximately, 100 tRNA modification enzymes have been identified with glucose-inhibited division (GidA) protein and MnmE being two of the enzymes studied. In Escherichia coli and Salmonella, GidA and MnmE bind together to form a functional complex responsible for the proper biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm⁵s²U34) of tRNAs. Studies have implicated this pathway in a major pathogenic regulatory mechanism as deletion of gidA and/or mnmE has attenuated several bacterial pathogens like Salmonella enterica serovar Typhimurium, Pseudomonas syringae, Aeromonas hydrophila, and many others. In this review, we summarize the potential role of the GidA/MnmE tRNA modification pathway in bacterial virulence, interactions with the host, and potential therapeutic strategies resulting from a greater understanding of this regulatory mechanism.</description><subject>Aeromonas hydrophila</subject><subject>Animals</subject><subject>Bacteria - pathogenicity</subject><subject>Bacterial infections</subject><subject>Bacterial Infections - metabolism</subject><subject>Bacterial Infections - pathology</subject><subject>Bacterial Physiological Phenomena</subject><subject>Bacterial Proteins - metabolism</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - pathogenicity</subject><subject>Escherichia coli - physiology</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Host-Pathogen Interactions</subject><subject>Humans</subject><subject>Pathogenesis</subject><subject>Pseudomonas syringae</subject><subject>Review</subject><subject>RNA, Transfer - metabolism</subject><subject>Salmonella enterica</subject><subject>Transfer RNA</subject><subject>Virulence</subject><subject>Virulence Factors - metabolism</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkctrFTEUh4MotrYu3UrATTejeT9cCJdSa6EqSF25CJk82lxmkmsyU2j_emdoLa0bV-fA-fg45_wAeIPRe0o1-pC2Y8McI6yIkM_APmaEdAgJ-fxRvwdetbZFiFDC9UuwRzjFSHC8D35NP75t4Fh8isnZKZUMQ769GUODp8lvoM0efs3jyUe4K1PIU7IDrGUIMGV4neo8hOwCLBH21k2hruOdna7KZcjtELyIdmjh9X09AD8_n1wcf-nOv5-eHW_OO8eYmjofsbBeheg5Vb30ygbNFI4qWtdroYXUse-DZ72LuLcSEY-ZF5hLKnrKCT0An-68u7kfg3fLmtUOZlfTaOuNKTaZp5OcrsxluTbLeyTBfBEc3Qtq-T2HNpkxNReGweZQ5mawJFJIpqX6PyqI1lxTtVrf_YNuy1zz8omVYpoQhlZhd0e5WlqrIT7sjZFZEzZPEl74t4-PfaD_Rkr_AFsloq0</recordid><startdate>20141010</startdate><enddate>20141010</enddate><creator>Shippy, Daniel C</creator><creator>Fadl, Amin A</creator><general>MDPI AG</general><general>MDPI</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>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>5PM</scope></search><sort><creationdate>20141010</creationdate><title>tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens</title><author>Shippy, Daniel C ; Fadl, Amin A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c448t-df16ad8efd538b7d8ae9481f8facb969679fbbed4bcf1ba702d14d615736b3523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Aeromonas hydrophila</topic><topic>Animals</topic><topic>Bacteria - pathogenicity</topic><topic>Bacterial infections</topic><topic>Bacterial Infections - metabolism</topic><topic>Bacterial Infections - pathology</topic><topic>Bacterial Physiological Phenomena</topic><topic>Bacterial Proteins - metabolism</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - pathogenicity</topic><topic>Escherichia coli - physiology</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>Host-Pathogen Interactions</topic><topic>Humans</topic><topic>Pathogenesis</topic><topic>Pseudomonas syringae</topic><topic>Review</topic><topic>RNA, Transfer - metabolism</topic><topic>Salmonella enterica</topic><topic>Transfer RNA</topic><topic>Virulence</topic><topic>Virulence Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shippy, Daniel C</creatorcontrib><creatorcontrib>Fadl, Amin A</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</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 Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</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>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shippy, Daniel C</au><au>Fadl, Amin A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2014-10-10</date><risdate>2014</risdate><volume>15</volume><issue>10</issue><spage>18267</spage><epage>18280</epage><pages>18267-18280</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modification is essential for translational efficiency. Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually with the tRNA. Approximately, 100 tRNA modification enzymes have been identified with glucose-inhibited division (GidA) protein and MnmE being two of the enzymes studied. In Escherichia coli and Salmonella, GidA and MnmE bind together to form a functional complex responsible for the proper biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm⁵s²U34) of tRNAs. Studies have implicated this pathway in a major pathogenic regulatory mechanism as deletion of gidA and/or mnmE has attenuated several bacterial pathogens like Salmonella enterica serovar Typhimurium, Pseudomonas syringae, Aeromonas hydrophila, and many others. In this review, we summarize the potential role of the GidA/MnmE tRNA modification pathway in bacterial virulence, interactions with the host, and potential therapeutic strategies resulting from a greater understanding of this regulatory mechanism.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>25310651</pmid><doi>10.3390/ijms151018267</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Aeromonas hydrophila Animals Bacteria - pathogenicity Bacterial infections Bacterial Infections - metabolism Bacterial Infections - pathology Bacterial Physiological Phenomena Bacterial Proteins - metabolism Enzymes Escherichia coli Escherichia coli - pathogenicity Escherichia coli - physiology Escherichia coli Proteins - metabolism GTP Phosphohydrolases - metabolism Host-Pathogen Interactions Humans Pathogenesis Pseudomonas syringae Review RNA, Transfer - metabolism Salmonella enterica Transfer RNA Virulence Virulence Factors - metabolism |
title | tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens |
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