Aminoacyl-tRNA synthetase-induced cleavage of tRNA
Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutamlnyl-tRNA synthetase destabilizes tRNAG in causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produ...
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| Veröffentlicht in: | Nucleic acids research 1992-04, Vol.20 (7), p.1523-1530 |
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| container_title | Nucleic acids research |
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| creator | Beresten, Sergey Jahn, Martina Söll, Dieter |
| description | Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutamlnyl-tRNA synthetase destabilizes tRNAG in causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNAGln species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule. |
| doi_str_mv | 10.1093/nar/20.7.1523 |
| format | Article |
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We have examined the phenomenon that upon complex formation E. coli glutamlnyl-tRNA synthetase destabilizes tRNAG in causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNAGln species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/20.7.1523</identifier><identifier>PMID: 1579445</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acyl-tRNA Synthetases - metabolism ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Ligases ; Magnesium - metabolism ; Molecular Sequence Data ; Mutation - genetics ; Nucleic Acid Conformation ; RNA, Transfer, Gln - chemistry ; RNA, Transfer, Gln - metabolism ; RNA, Transfer, Trp - chemistry ; RNA, Transfer, Trp - metabolism</subject><ispartof>Nucleic acids research, 1992-04, Vol.20 (7), p.1523-1530</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4253-bd5699d30ef2341b79e477cd888c79777eb2ed288cf6e74d7737d78fe49096c73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC312233/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC312233/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5227996$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1579445$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Beresten, Sergey</creatorcontrib><creatorcontrib>Jahn, Martina</creatorcontrib><creatorcontrib>Söll, Dieter</creatorcontrib><title>Aminoacyl-tRNA synthetase-induced cleavage of tRNA</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutamlnyl-tRNA synthetase destabilizes tRNAG in causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNAGln species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.</description><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Ligases</subject><subject>Magnesium - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>Nucleic Acid Conformation</subject><subject>RNA, Transfer, Gln - chemistry</subject><subject>RNA, Transfer, Gln - metabolism</subject><subject>RNA, Transfer, Trp - chemistry</subject><subject>RNA, Transfer, Trp - metabolism</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1PGzEQhq2KigboscdKOSBum9gee2d94BAQX1LaShWtol4sx56FLZtdsDeI_Hs2ShTaE6fR6H3m82Xsi-AjwQ2MGxfHko9wJLSED2wgIJeZMrncYwMOXGeCq-ITO0jpL-dCCa322b7QaJTSAyYni6ppnV_VWffz-2SYVk13T51LlFVNWHoKQ1-Te3Z3NGzL4Zo5Yh9LVyf6vI2H7Nflxe35dTb9cXVzPplmXkkN2Tzo3JgAnEoJSszRkEL0oSgKjwYRaS4pyD4rc0IVEAEDFiUpw03uEQ7Z6abv43K-oOCp6aKr7WOsFi6ubOsq-7_SVPf2rn22IKQE6OtPtvWxfVpS6uyiSp7q2jXULpNFaQCKAt8FhQHV_1a8D-baKIB1x2wD-timFKncbS24Xbtme9es5Bbt2rWe__rvqW_0xqZeP97qLnlXl9E1vko7TEuJxuRvY6vU0ctOdvHB5v13tb2e_bG_Ocz0t7OZlfAKcg-tzA</recordid><startdate>19920411</startdate><enddate>19920411</enddate><creator>Beresten, Sergey</creator><creator>Jahn, Martina</creator><creator>Söll, Dieter</creator><general>Oxford University Press</general><scope>BSCLL</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>7TM</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19920411</creationdate><title>Aminoacyl-tRNA synthetase-induced cleavage of tRNA</title><author>Beresten, Sergey ; Jahn, Martina ; Söll, Dieter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4253-bd5699d30ef2341b79e477cd888c79777eb2ed288cf6e74d7737d78fe49096c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acyl-tRNA Synthetases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Ligases</topic><topic>Magnesium - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutation - genetics</topic><topic>Nucleic Acid Conformation</topic><topic>RNA, Transfer, Gln - chemistry</topic><topic>RNA, Transfer, Gln - metabolism</topic><topic>RNA, Transfer, Trp - chemistry</topic><topic>RNA, Transfer, Trp - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Beresten, Sergey</creatorcontrib><creatorcontrib>Jahn, Martina</creatorcontrib><creatorcontrib>Söll, Dieter</creatorcontrib><collection>Istex</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>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Beresten, Sergey</au><au>Jahn, Martina</au><au>Söll, Dieter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aminoacyl-tRNA synthetase-induced cleavage of tRNA</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1992-04-11</date><risdate>1992</risdate><volume>20</volume><issue>7</issue><spage>1523</spage><epage>1530</epage><pages>1523-1530</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutamlnyl-tRNA synthetase destabilizes tRNAG in causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNAGln species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>1579445</pmid><doi>10.1093/nar/20.7.1523</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nucleic acids research, 1992-04, Vol.20 (7), p.1523-1530 |
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| subjects | Amino Acyl-tRNA Synthetases - metabolism Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Kinetics Ligases Magnesium - metabolism Molecular Sequence Data Mutation - genetics Nucleic Acid Conformation RNA, Transfer, Gln - chemistry RNA, Transfer, Gln - metabolism RNA, Transfer, Trp - chemistry RNA, Transfer, Trp - metabolism |
| title | Aminoacyl-tRNA synthetase-induced cleavage of tRNA |
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