Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E.coli
Selenocysteine-incorporating tRNA(Sec)(UCA), the product of selC, was isolated from E.coli and aminoacylated with serine. The equilibrium dissociation constant for the interaction of Ser-tRNA(Sec)(UCA) with elongation factor Tu.GTP was determined to be 5.0 +/- 2.5 x 10(-8) M. Compared with the disso...
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| Veröffentlicht in: | Nucleic acids research 1990-02, Vol.18 (3), p.487-491 |
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| creator | Förster, C Ott, G Forchhammer, K Sprinzl, M |
| description | Selenocysteine-incorporating tRNA(Sec)(UCA), the product of selC, was isolated from E.coli and aminoacylated with serine. The equilibrium dissociation constant for the interaction of Ser-tRNA(Sec)(UCA) with elongation factor Tu.GTP was determined to be 5.0 +/- 2.5 x 10(-8) M. Compared with the dissociation constants of the two elongator Ser-tRNA(Ser) species (Kd = 7 x 10(-10) M), the selenocysteine-incorporating UGA suppressor tRNA has an almost hundred fold weaker affinity for EF-Tu.GTP. This suggests a mechanism by which the Ser-tRNA(Sec) is prevented in recognition of UGA codons. This tRNA is not bound to EF-Tu.GTP and is converted to selenocysteinyl-tRNA(Sec). We also demonstrate the lack of an efficient interaction of Sec-tRNA(Sec)(UCA) with EF-Tu.GTP. The results of this work are in support of a mechanism by which the selenocysteine incorporation at UGA nonsense codons is mediated by an elongation factor other than EF-Tu.GTP. |
| doi_str_mv | 10.1093/nar/18.3.487 |
| format | Article |
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The equilibrium dissociation constant for the interaction of Ser-tRNA(Sec)(UCA) with elongation factor Tu.GTP was determined to be 5.0 +/- 2.5 x 10(-8) M. Compared with the dissociation constants of the two elongator Ser-tRNA(Ser) species (Kd = 7 x 10(-10) M), the selenocysteine-incorporating UGA suppressor tRNA has an almost hundred fold weaker affinity for EF-Tu.GTP. This suggests a mechanism by which the Ser-tRNA(Sec) is prevented in recognition of UGA codons. This tRNA is not bound to EF-Tu.GTP and is converted to selenocysteinyl-tRNA(Sec). We also demonstrate the lack of an efficient interaction of Sec-tRNA(Sec)(UCA) with EF-Tu.GTP. The results of this work are in support of a mechanism by which the selenocysteine incorporation at UGA nonsense codons is mediated by an elongation factor other than EF-Tu.GTP.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/18.3.487</identifier><identifier>PMID: 2408012</identifier><language>eng</language><publisher>England</publisher><subject>Chromatography, Affinity ; Codon ; Electrophoresis, Gel, Two-Dimensional ; Escherichia coli - metabolism ; Gene Expression ; Guanosine Triphosphate - metabolism ; Peptide Elongation Factor Tu - metabolism ; RNA, Transfer, Amino Acid-Specific - metabolism</subject><ispartof>Nucleic acids research, 1990-02, Vol.18 (3), p.487-491</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c286t-1690867ba588480e52495c2268b63039be77831d5297cee96961a32b5c9db5523</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/PMC333452/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC333452/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2408012$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Förster, C</creatorcontrib><creatorcontrib>Ott, G</creatorcontrib><creatorcontrib>Forchhammer, K</creatorcontrib><creatorcontrib>Sprinzl, M</creatorcontrib><title>Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E.coli</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Selenocysteine-incorporating tRNA(Sec)(UCA), the product of selC, was isolated from E.coli and aminoacylated with serine. The equilibrium dissociation constant for the interaction of Ser-tRNA(Sec)(UCA) with elongation factor Tu.GTP was determined to be 5.0 +/- 2.5 x 10(-8) M. Compared with the dissociation constants of the two elongator Ser-tRNA(Ser) species (Kd = 7 x 10(-10) M), the selenocysteine-incorporating UGA suppressor tRNA has an almost hundred fold weaker affinity for EF-Tu.GTP. This suggests a mechanism by which the Ser-tRNA(Sec) is prevented in recognition of UGA codons. This tRNA is not bound to EF-Tu.GTP and is converted to selenocysteinyl-tRNA(Sec). We also demonstrate the lack of an efficient interaction of Sec-tRNA(Sec)(UCA) with EF-Tu.GTP. The results of this work are in support of a mechanism by which the selenocysteine incorporation at UGA nonsense codons is mediated by an elongation factor other than EF-Tu.GTP.</description><subject>Chromatography, Affinity</subject><subject>Codon</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Escherichia coli - metabolism</subject><subject>Gene Expression</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Peptide Elongation Factor Tu - metabolism</subject><subject>RNA, Transfer, Amino Acid-Specific - metabolism</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LYzEUQMOg1Oq4m62QlStfzfdLFi5EqiOIgjjgLuSl97WR16Qm6Qz991O1iLOaVRb3nMsNB6EflEwoMfw8unxO9YRPhG6_oTHlijXCKLaHxoQT2VAi9AE6LOWFECqoFCM0YoJoQtkYPd_GCtn5GlLEqccOFxggJr8pFUKEJkSf8iplV0Oc4_p4f4n_hLrAMKQ4d-9av9VTxk9r3Oe0xNOJT0P4jvZ7NxQ43r1H6Nf19OnqZ3P3cHN7dXnXeKZVbagyRKu2c1JroQlIJoz0jCndKU646aBtNaczyUzrAYwyijrOOunNrJOS8SN08bF3te6WMPMQa3aDXeWwdHljkwv230kMCztPvy3nXLz7pzs_p9c1lGqXoXgYBhchrYttjZJKa_JfkBquuJZv4NkH6HMqJUP_eQwl9q2Y3RazVFtut8W2-MnXD3zCu0T8L0Vckik</recordid><startdate>19900211</startdate><enddate>19900211</enddate><creator>Förster, C</creator><creator>Ott, G</creator><creator>Forchhammer, K</creator><creator>Sprinzl, M</creator><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>7TM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19900211</creationdate><title>Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E.coli</title><author>Förster, C ; Ott, G ; Forchhammer, K ; Sprinzl, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c286t-1690867ba588480e52495c2268b63039be77831d5297cee96961a32b5c9db5523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Chromatography, Affinity</topic><topic>Codon</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Escherichia coli - metabolism</topic><topic>Gene Expression</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Peptide Elongation Factor Tu - metabolism</topic><topic>RNA, Transfer, Amino Acid-Specific - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Förster, C</creatorcontrib><creatorcontrib>Ott, G</creatorcontrib><creatorcontrib>Forchhammer, K</creatorcontrib><creatorcontrib>Sprinzl, M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</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>Förster, C</au><au>Ott, G</au><au>Forchhammer, K</au><au>Sprinzl, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E.coli</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1990-02-11</date><risdate>1990</risdate><volume>18</volume><issue>3</issue><spage>487</spage><epage>491</epage><pages>487-491</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Selenocysteine-incorporating tRNA(Sec)(UCA), the product of selC, was isolated from E.coli and aminoacylated with serine. The equilibrium dissociation constant for the interaction of Ser-tRNA(Sec)(UCA) with elongation factor Tu.GTP was determined to be 5.0 +/- 2.5 x 10(-8) M. Compared with the dissociation constants of the two elongator Ser-tRNA(Ser) species (Kd = 7 x 10(-10) M), the selenocysteine-incorporating UGA suppressor tRNA has an almost hundred fold weaker affinity for EF-Tu.GTP. This suggests a mechanism by which the Ser-tRNA(Sec) is prevented in recognition of UGA codons. This tRNA is not bound to EF-Tu.GTP and is converted to selenocysteinyl-tRNA(Sec). We also demonstrate the lack of an efficient interaction of Sec-tRNA(Sec)(UCA) with EF-Tu.GTP. The results of this work are in support of a mechanism by which the selenocysteine incorporation at UGA nonsense codons is mediated by an elongation factor other than EF-Tu.GTP.</abstract><cop>England</cop><pmid>2408012</pmid><doi>10.1093/nar/18.3.487</doi><tpages>5</tpages></addata></record> |
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| ispartof | Nucleic acids research, 1990-02, Vol.18 (3), p.487-491 |
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| language | eng |
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| source | MEDLINE; PubMed Central; Oxford University Press Journals Digital Archive Legacy |
| subjects | Chromatography, Affinity Codon Electrophoresis, Gel, Two-Dimensional Escherichia coli - metabolism Gene Expression Guanosine Triphosphate - metabolism Peptide Elongation Factor Tu - metabolism RNA, Transfer, Amino Acid-Specific - metabolism |
| title | Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E.coli |
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