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Interactions Between Natural Polyamines and tRNA: An15N NMR Analysis
15N NMR spectroscopy was used to explore the interactions between natural polyamines and Escherichia coli tRNA. It was found that when tRNA is added to solutions of15N-labeled spermine or spermidine, there is a considerable decrease in the relative heights of the -NH+ 2-resonances with respect to th...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 1992-10, Vol.89 (19), p.9186-9190 |
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container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Frydman, Lucio Rossomando, Pedro C. Frydman, Veronica Fernandez, Claudio O. Frydman, Benjamin Samejima, Keijo |
description | 15N NMR spectroscopy was used to explore the interactions between natural polyamines and Escherichia coli tRNA. It was found that when tRNA is added to solutions of15N-labeled spermine or spermidine, there is a considerable decrease in the relative heights of the -NH+
2-resonances with respect to the signals arising from the -NH+
3groups. The presence of tRNA was also found to reduce the longitudinal relaxation times T1of the nitrogens, mainly those of the -NH+
2- groups. The longitudinal relaxation times of the nitrogens were used to characterize the temperature dependence of the binding, and they allowed us to calculate the activation energies that determine the correlation times of amino groups in the presence of tRNA. Both the thermodynamic and the relaxation results indicate that (i) spermine binds more strongly to tRNA than spermidine does and (ii) within each of these molecules the -NH+
2- groups bind more strongly to tRNA than the more electropositive -NH+
3moieties. This specificity suggests that the interaction between polyamines and tRNA cannot be described exclusively in terms of electrostatic forces and that other interactions (most likely, hydrogen bonding) are very important for establishing the polyamine-tRNA link. Some of the factors that may conspire against the binding of -NH+
3groups to tRNA are briefly discussed. |
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2-resonances with respect to the signals arising from the -NH+
3groups. The presence of tRNA was also found to reduce the longitudinal relaxation times T1of the nitrogens, mainly those of the -NH+
2- groups. The longitudinal relaxation times of the nitrogens were used to characterize the temperature dependence of the binding, and they allowed us to calculate the activation energies that determine the correlation times of amino groups in the presence of tRNA. Both the thermodynamic and the relaxation results indicate that (i) spermine binds more strongly to tRNA than spermidine does and (ii) within each of these molecules the -NH+
2- groups bind more strongly to tRNA than the more electropositive -NH+
3moieties. This specificity suggests that the interaction between polyamines and tRNA cannot be described exclusively in terms of electrostatic forces and that other interactions (most likely, hydrogen bonding) are very important for establishing the polyamine-tRNA link. Some of the factors that may conspire against the binding of -NH+
3groups to tRNA are briefly discussed.</description><identifier>ISSN: 0027-8424</identifier><language>eng</language><publisher>National Academy of Sciences of the United States of America</publisher><subject>Activation energy ; Biochemistry ; Drug interactions ; Molecules ; Nitrogen ; Nuclear interactions ; Nucleic acids ; Polyamines ; Relaxation time ; Transfer RNA</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1992-10, Vol.89 (19), p.9186-9190</ispartof><rights>Copyright 1992 The National Academy of Sciences of the United States of America</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2360357$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2360357$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,58238,58471</link.rule.ids></links><search><creatorcontrib>Frydman, Lucio</creatorcontrib><creatorcontrib>Rossomando, Pedro C.</creatorcontrib><creatorcontrib>Frydman, Veronica</creatorcontrib><creatorcontrib>Fernandez, Claudio O.</creatorcontrib><creatorcontrib>Frydman, Benjamin</creatorcontrib><creatorcontrib>Samejima, Keijo</creatorcontrib><title>Interactions Between Natural Polyamines and tRNA: An15N NMR Analysis</title><title>Proceedings of the National Academy of Sciences - PNAS</title><description>15N NMR spectroscopy was used to explore the interactions between natural polyamines and Escherichia coli tRNA. It was found that when tRNA is added to solutions of15N-labeled spermine or spermidine, there is a considerable decrease in the relative heights of the -NH+
2-resonances with respect to the signals arising from the -NH+
3groups. The presence of tRNA was also found to reduce the longitudinal relaxation times T1of the nitrogens, mainly those of the -NH+
2- groups. The longitudinal relaxation times of the nitrogens were used to characterize the temperature dependence of the binding, and they allowed us to calculate the activation energies that determine the correlation times of amino groups in the presence of tRNA. Both the thermodynamic and the relaxation results indicate that (i) spermine binds more strongly to tRNA than spermidine does and (ii) within each of these molecules the -NH+
2- groups bind more strongly to tRNA than the more electropositive -NH+
3moieties. This specificity suggests that the interaction between polyamines and tRNA cannot be described exclusively in terms of electrostatic forces and that other interactions (most likely, hydrogen bonding) are very important for establishing the polyamine-tRNA link. Some of the factors that may conspire against the binding of -NH+
3groups to tRNA are briefly discussed.</description><subject>Activation energy</subject><subject>Biochemistry</subject><subject>Drug interactions</subject><subject>Molecules</subject><subject>Nitrogen</subject><subject>Nuclear interactions</subject><subject>Nucleic acids</subject><subject>Polyamines</subject><subject>Relaxation time</subject><subject>Transfer RNA</subject><issn>0027-8424</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNpjYeA0MDAy17UwMTLhYOAqLs4yMDCwNLUw4GRw8cwrSS1KTC7JzM8rVnBKLSlPTc1T8EssKS1KzFEIyM-pTMzNzEstVkjMS1EoCfJztFJwzDM09VPw8w0CshJzKoszi3kYWNMSc4pTeaE0N4OMm2uIs4duVnFJflF8QVFmbmJRZbyRsZmBsam5MQFpACnVM80</recordid><startdate>19921001</startdate><enddate>19921001</enddate><creator>Frydman, Lucio</creator><creator>Rossomando, Pedro C.</creator><creator>Frydman, Veronica</creator><creator>Fernandez, Claudio O.</creator><creator>Frydman, Benjamin</creator><creator>Samejima, Keijo</creator><general>National Academy of Sciences of the United States of America</general><scope/></search><sort><creationdate>19921001</creationdate><title>Interactions Between Natural Polyamines and tRNA: An15N NMR Analysis</title><author>Frydman, Lucio ; Rossomando, Pedro C. ; Frydman, Veronica ; Fernandez, Claudio O. ; Frydman, Benjamin ; Samejima, Keijo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-jstor_primary_23603573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Activation energy</topic><topic>Biochemistry</topic><topic>Drug interactions</topic><topic>Molecules</topic><topic>Nitrogen</topic><topic>Nuclear interactions</topic><topic>Nucleic acids</topic><topic>Polyamines</topic><topic>Relaxation time</topic><topic>Transfer RNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frydman, Lucio</creatorcontrib><creatorcontrib>Rossomando, Pedro C.</creatorcontrib><creatorcontrib>Frydman, Veronica</creatorcontrib><creatorcontrib>Fernandez, Claudio O.</creatorcontrib><creatorcontrib>Frydman, Benjamin</creatorcontrib><creatorcontrib>Samejima, Keijo</creatorcontrib><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frydman, Lucio</au><au>Rossomando, Pedro C.</au><au>Frydman, Veronica</au><au>Fernandez, Claudio O.</au><au>Frydman, Benjamin</au><au>Samejima, Keijo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions Between Natural Polyamines and tRNA: An15N NMR Analysis</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><date>1992-10-01</date><risdate>1992</risdate><volume>89</volume><issue>19</issue><spage>9186</spage><epage>9190</epage><pages>9186-9190</pages><issn>0027-8424</issn><abstract>15N NMR spectroscopy was used to explore the interactions between natural polyamines and Escherichia coli tRNA. It was found that when tRNA is added to solutions of15N-labeled spermine or spermidine, there is a considerable decrease in the relative heights of the -NH+
2-resonances with respect to the signals arising from the -NH+
3groups. The presence of tRNA was also found to reduce the longitudinal relaxation times T1of the nitrogens, mainly those of the -NH+
2- groups. The longitudinal relaxation times of the nitrogens were used to characterize the temperature dependence of the binding, and they allowed us to calculate the activation energies that determine the correlation times of amino groups in the presence of tRNA. Both the thermodynamic and the relaxation results indicate that (i) spermine binds more strongly to tRNA than spermidine does and (ii) within each of these molecules the -NH+
2- groups bind more strongly to tRNA than the more electropositive -NH+
3moieties. This specificity suggests that the interaction between polyamines and tRNA cannot be described exclusively in terms of electrostatic forces and that other interactions (most likely, hydrogen bonding) are very important for establishing the polyamine-tRNA link. Some of the factors that may conspire against the binding of -NH+
3groups to tRNA are briefly discussed.</abstract><pub>National Academy of Sciences of the United States of America</pub></addata></record> |
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source | PubMed (Medline); JSTOR |
subjects | Activation energy Biochemistry Drug interactions Molecules Nitrogen Nuclear interactions Nucleic acids Polyamines Relaxation time Transfer RNA |
title | Interactions Between Natural Polyamines and tRNA: An15N NMR Analysis |
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