Binding of protein synthesis initiation factor 4E to oligoribonucleotides: effects of cap accessibility and secondary structure
The binding of rabbit globin mRNA to the 25-kDa cap binding protein eIF-4E from human erythrocytes was found to be 5.3-fold stronger than the binding of the cap analogue m7GpppG to eIF-4E [Gross et al. (1990) Biochemistry 29, 5008-5012]. In order to investigate whether this effect is due to the long...
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| Veröffentlicht in: | Biochemistry (Easton) 1992-02, Vol.31 (5), p.1427-1432 |
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| creator | Carberry, Susan E Friedland, Diana E Rhoads, Robert E Goss, Dixie J |
| description | The binding of rabbit globin mRNA to the 25-kDa cap binding protein eIF-4E from human erythrocytes was found to be 5.3-fold stronger than the binding of the cap analogue m7GpppG to eIF-4E [Gross et al. (1990) Biochemistry 29, 5008-5012]. In order to investigate whether this effect is due to the longer sequence of nucleotides in globin mRNA or to other features such as cap accessibility or secondary structure, oligoribonucleotide analogues of rabbit alpha-globin mRNA were synthesized by T7 RNA polymerase from a synthetic oligodeoxynucleotide template in the presence of m7GpppG; these oligoribonucleotide analogues possess varying degrees of cap accessibility and secondary structure. Equilibrium association constants for the interaction of these oligoribonucleotides and purified human erythrocyte eIF-4E were obtained from direct fluorescence titration experiments. The data indicate that while the presence of the m7G cap is required for efficient recognition by eIF-4E, the cap need not be completely sterically accessible, since other structural features within the mRNA also influence binding. |
| doi_str_mv | 10.1021/bi00120a020 |
| format | Article |
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(1990) Biochemistry 29, 5008-5012]. In order to investigate whether this effect is due to the longer sequence of nucleotides in globin mRNA or to other features such as cap accessibility or secondary structure, oligoribonucleotide analogues of rabbit alpha-globin mRNA were synthesized by T7 RNA polymerase from a synthetic oligodeoxynucleotide template in the presence of m7GpppG; these oligoribonucleotide analogues possess varying degrees of cap accessibility and secondary structure. Equilibrium association constants for the interaction of these oligoribonucleotides and purified human erythrocyte eIF-4E were obtained from direct fluorescence titration experiments. The data indicate that while the presence of the m7G cap is required for efficient recognition by eIF-4E, the cap need not be completely sterically accessible, since other structural features within the mRNA also influence binding.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00120a020</identifier><identifier>PMID: 1737000</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Base Sequence ; Biological and medical sciences ; DNA-Directed RNA Polymerases - chemistry ; Erythrocytes - chemistry ; Eukaryotic Initiation Factor-4E ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; Globins - chemistry ; Humans ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides - chemistry ; Peptide Initiation Factors - chemistry ; Peptide Initiation Factors - genetics ; Protein Binding ; Rabbits ; RNA Caps - chemistry ; Structure-Activity Relationship ; Translation. Translation factors. Protein processing ; Viral Proteins</subject><ispartof>Biochemistry (Easton), 1992-02, Vol.31 (5), p.1427-1432</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a414t-53e2ab707dfeab74cf00f92fee870abadca1c9c0851550ef3289bfa0a65da8c83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00120a020$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00120a020$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5383613$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1737000$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carberry, Susan E</creatorcontrib><creatorcontrib>Friedland, Diana E</creatorcontrib><creatorcontrib>Rhoads, Robert E</creatorcontrib><creatorcontrib>Goss, Dixie J</creatorcontrib><title>Binding of protein synthesis initiation factor 4E to oligoribonucleotides: effects of cap accessibility and secondary structure</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The binding of rabbit globin mRNA to the 25-kDa cap binding protein eIF-4E from human erythrocytes was found to be 5.3-fold stronger than the binding of the cap analogue m7GpppG to eIF-4E [Gross et al. (1990) Biochemistry 29, 5008-5012]. In order to investigate whether this effect is due to the longer sequence of nucleotides in globin mRNA or to other features such as cap accessibility or secondary structure, oligoribonucleotide analogues of rabbit alpha-globin mRNA were synthesized by T7 RNA polymerase from a synthetic oligodeoxynucleotide template in the presence of m7GpppG; these oligoribonucleotide analogues possess varying degrees of cap accessibility and secondary structure. Equilibrium association constants for the interaction of these oligoribonucleotides and purified human erythrocyte eIF-4E were obtained from direct fluorescence titration experiments. The data indicate that while the presence of the m7G cap is required for efficient recognition by eIF-4E, the cap need not be completely sterically accessible, since other structural features within the mRNA also influence binding.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>DNA-Directed RNA Polymerases - chemistry</subject><subject>Erythrocytes - chemistry</subject><subject>Eukaryotic Initiation Factor-4E</subject><subject>Fluorescence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Globins - chemistry</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Oligoribonucleotides - chemistry</subject><subject>Peptide Initiation Factors - chemistry</subject><subject>Peptide Initiation Factors - genetics</subject><subject>Protein Binding</subject><subject>Rabbits</subject><subject>RNA Caps - chemistry</subject><subject>Structure-Activity Relationship</subject><subject>Translation. Translation factors. Protein processing</subject><subject>Viral Proteins</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1rFEEQxQdR4ho9eRb6IOYgo9Uz0_ORm4YYxQUFo9empqc6dpztXrt6IHvyX7fDLtGD4Kl4vB-PqnpF8VTCKwmVfD06AFkBQgX3ipVUFZTNMKj7xQoA2rIaWnhYPGK-zrKBrjkqjmRXd1mtil9vnZ-cvxLBim0MiZwXvPPpO7Fj4bxLDpMLXlg0KUTRnIsURJjdVYhuDH4xM4XkJuJTQdaSSXwbZXAr0BhidqObXdoJ9JNgMsFPGHeCU1xMWiI9Lh5YnJmeHOZx8fXd-eXZ-3L96eLD2Zt1iY1sUqlqqnDsoJss5dkYC2CHyhL1HeCIk0FpBgO9kkoB2brqh9EiYKsm7E1fHxcv9rn5yJ8LcdIbx4bmGT2FhXVX9dCo7v-gbFuQXasy-HIPmhiYI1m9jW6Tj9MS9G0v-q9eMv3sELuMG5r-sPsisv_84CMbnG1EbxzfYaru61bWGSv3mONEN3c2xh-6zUlKX37-otf9x6b6tpb6IvMnex4N6-uwRJ-f_M8FfwOgDLNP</recordid><startdate>19920211</startdate><enddate>19920211</enddate><creator>Carberry, Susan E</creator><creator>Friedland, Diana E</creator><creator>Rhoads, Robert E</creator><creator>Goss, Dixie J</creator><general>American Chemical Society</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19920211</creationdate><title>Binding of protein synthesis initiation factor 4E to oligoribonucleotides: effects of cap accessibility and secondary structure</title><author>Carberry, Susan E ; Friedland, Diana E ; Rhoads, Robert E ; Goss, Dixie J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a414t-53e2ab707dfeab74cf00f92fee870abadca1c9c0851550ef3289bfa0a65da8c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>DNA-Directed RNA Polymerases - chemistry</topic><topic>Erythrocytes - chemistry</topic><topic>Eukaryotic Initiation Factor-4E</topic><topic>Fluorescence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Globins - chemistry</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Oligoribonucleotides - chemistry</topic><topic>Peptide Initiation Factors - chemistry</topic><topic>Peptide Initiation Factors - genetics</topic><topic>Protein Binding</topic><topic>Rabbits</topic><topic>RNA Caps - chemistry</topic><topic>Structure-Activity Relationship</topic><topic>Translation. Translation factors. Protein processing</topic><topic>Viral Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carberry, Susan E</creatorcontrib><creatorcontrib>Friedland, Diana E</creatorcontrib><creatorcontrib>Rhoads, Robert E</creatorcontrib><creatorcontrib>Goss, Dixie J</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>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carberry, Susan E</au><au>Friedland, Diana E</au><au>Rhoads, Robert E</au><au>Goss, Dixie J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of protein synthesis initiation factor 4E to oligoribonucleotides: effects of cap accessibility and secondary structure</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1992-02-11</date><risdate>1992</risdate><volume>31</volume><issue>5</issue><spage>1427</spage><epage>1432</epage><pages>1427-1432</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The binding of rabbit globin mRNA to the 25-kDa cap binding protein eIF-4E from human erythrocytes was found to be 5.3-fold stronger than the binding of the cap analogue m7GpppG to eIF-4E [Gross et al. (1990) Biochemistry 29, 5008-5012]. In order to investigate whether this effect is due to the longer sequence of nucleotides in globin mRNA or to other features such as cap accessibility or secondary structure, oligoribonucleotide analogues of rabbit alpha-globin mRNA were synthesized by T7 RNA polymerase from a synthetic oligodeoxynucleotide template in the presence of m7GpppG; these oligoribonucleotide analogues possess varying degrees of cap accessibility and secondary structure. Equilibrium association constants for the interaction of these oligoribonucleotides and purified human erythrocyte eIF-4E were obtained from direct fluorescence titration experiments. The data indicate that while the presence of the m7G cap is required for efficient recognition by eIF-4E, the cap need not be completely sterically accessible, since other structural features within the mRNA also influence binding.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1737000</pmid><doi>10.1021/bi00120a020</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Base Sequence Biological and medical sciences DNA-Directed RNA Polymerases - chemistry Erythrocytes - chemistry Eukaryotic Initiation Factor-4E Fluorescence Fundamental and applied biological sciences. Psychology Globins - chemistry Humans Molecular and cellular biology Molecular genetics Molecular Sequence Data Nucleic Acid Conformation Oligoribonucleotides - chemistry Peptide Initiation Factors - chemistry Peptide Initiation Factors - genetics Protein Binding Rabbits RNA Caps - chemistry Structure-Activity Relationship Translation. Translation factors. Protein processing Viral Proteins |
| title | Binding of protein synthesis initiation factor 4E to oligoribonucleotides: effects of cap accessibility and secondary structure |
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