Structure of functional a salina - E Coli hybrid ribosome by electron microscopy
Small 40S Artemia salina and large 50S Escherichia coli ribosomal subunits can be assembled into 73S hybrid monosomes active in model assays for protein synthesis. The reciprocal combination–small 30S E coli and large 60S A salina–fails to form hybrids. The 73S hybrid particles strongly resemble hom...
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| Veröffentlicht in: | Journal of supramolecular structure 1979, Vol.10 (4), p.397-404 |
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| container_title | Journal of supramolecular structure |
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| creator | Boublik, M. Wydro, R. M. Hellmann, W. Jenkins, F. |
| description | Small 40S Artemia salina and large 50S Escherichia coli ribosomal subunits can be assembled into 73S hybrid monosomes active in model assays for protein synthesis. The reciprocal combination–small 30S E coli and large 60S A salina–fails to form hybrids. The 73S hybrid particles strongly resemble homologous 70S E coli and 80S A salina monosomes. The morphologic differences between the corresponding eukaryotic and prokaryotic ribosomal particles, established by electron microscopy, do not significantly affect the assembly and mutual orientation of 40S A salina and 50S E coli subunits in the heterologous monosome. The fact that the structure of the interface, the supposed site of protein synthesis, is preserved in the active hybrid implies that retention or loss of biologic activity of hybrid ribosomes is determined by the extent of conformational changes in the interface. |
| doi_str_mv | 10.1002/jss.400100403 |
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The fact that the structure of the interface, the supposed site of protein synthesis, is preserved in the active hybrid implies that retention or loss of biologic activity of hybrid ribosomes is determined by the extent of conformational changes in the interface.</description><identifier>ISSN: 0091-7419</identifier><identifier>EISSN: 1547-9366</identifier><identifier>DOI: 10.1002/jss.400100403</identifier><identifier>PMID: 390251</identifier><language>eng</language><publisher>New York: Alan R. Liss, Inc</publisher><subject>Animals ; Artemia ; electron microscopy ; Escherichia coli - metabolism ; Escherichia coli - ultrastructure ; hybrid ribosome ; Microscopy, Electron ; Phenylalanine - metabolism ; Protein Biosynthesis ; ribosome structure ; Ribosomes - metabolism ; Ribosomes - ultrastructure ; RNA, Transfer - metabolism</subject><ispartof>Journal of supramolecular structure, 1979, Vol.10 (4), p.397-404</ispartof><rights>Copyright © 1979 Alan R. 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M.</creatorcontrib><creatorcontrib>Hellmann, W.</creatorcontrib><creatorcontrib>Jenkins, F.</creatorcontrib><title>Structure of functional a salina - E Coli hybrid ribosome by electron microscopy</title><title>Journal of supramolecular structure</title><addtitle>J. Supramol. Struct</addtitle><description>Small 40S Artemia salina and large 50S Escherichia coli ribosomal subunits can be assembled into 73S hybrid monosomes active in model assays for protein synthesis. The reciprocal combination–small 30S E coli and large 60S A salina–fails to form hybrids. The 73S hybrid particles strongly resemble homologous 70S E coli and 80S A salina monosomes. The morphologic differences between the corresponding eukaryotic and prokaryotic ribosomal particles, established by electron microscopy, do not significantly affect the assembly and mutual orientation of 40S A salina and 50S E coli subunits in the heterologous monosome. The fact that the structure of the interface, the supposed site of protein synthesis, is preserved in the active hybrid implies that retention or loss of biologic activity of hybrid ribosomes is determined by the extent of conformational changes in the interface.</description><subject>Animals</subject><subject>Artemia</subject><subject>electron microscopy</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli - ultrastructure</subject><subject>hybrid ribosome</subject><subject>Microscopy, Electron</subject><subject>Phenylalanine - metabolism</subject><subject>Protein Biosynthesis</subject><subject>ribosome structure</subject><subject>Ribosomes - metabolism</subject><subject>Ribosomes - ultrastructure</subject><subject>RNA, Transfer - metabolism</subject><issn>0091-7419</issn><issn>1547-9366</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLtPwzAQxi3EqxRGNgZPbIFz_EpGVN5CgNQiRstJbGFI4mIngvz3BLWqmFjuTrrfffruQ-iYwBkBSM_fYzxjAOPMgG6hCeFMJjkVYhtNAHKSSEbyfXQQ4zsAJZCxPbRLc0g5maDneRf6suuDwd5i27dl53yra6xx1LVrNU7wFZ752uG3oQiuwsEVPvrG4GLApjZlF3yLG1cGH0u_HA7RjtV1NEfrPkUv11eL2W3y8HRzN7t4SEoqKU0qC5SDsBWlujA6KwQU4w-akVRa0KwSprSEpcJwlo8lMxRsJnhqORW80nSKTle6y-A_exM71bhYmrrWrfF9VJJlI0nYCCYr8NdhDMaqZXCNDoMioH4DVGOAahPgyJ-shfuiMdWGXiU2ruVq_eVqM_yvpe7n87_CayMuduZ7c6nDhxKSSq5eH2_UJbDFK7-kStIf1_yKLA</recordid><startdate>1979</startdate><enddate>1979</enddate><creator>Boublik, M.</creator><creator>Wydro, R. 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M. ; Hellmann, W. ; Jenkins, F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3733-df03506fd33abea8b60b001a4127f0a4d6ecf1426e5496e58e30f8652f5365da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Animals</topic><topic>Artemia</topic><topic>electron microscopy</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli - ultrastructure</topic><topic>hybrid ribosome</topic><topic>Microscopy, Electron</topic><topic>Phenylalanine - metabolism</topic><topic>Protein Biosynthesis</topic><topic>ribosome structure</topic><topic>Ribosomes - metabolism</topic><topic>Ribosomes - ultrastructure</topic><topic>RNA, Transfer - metabolism</topic><toplevel>online_resources</toplevel><creatorcontrib>Boublik, M.</creatorcontrib><creatorcontrib>Wydro, R. M.</creatorcontrib><creatorcontrib>Hellmann, W.</creatorcontrib><creatorcontrib>Jenkins, F.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of supramolecular structure</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boublik, M.</au><au>Wydro, R. M.</au><au>Hellmann, W.</au><au>Jenkins, F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of functional a salina - E Coli hybrid ribosome by electron microscopy</atitle><jtitle>Journal of supramolecular structure</jtitle><addtitle>J. Supramol. 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The fact that the structure of the interface, the supposed site of protein synthesis, is preserved in the active hybrid implies that retention or loss of biologic activity of hybrid ribosomes is determined by the extent of conformational changes in the interface.</abstract><cop>New York</cop><pub>Alan R. Liss, Inc</pub><pmid>390251</pmid><doi>10.1002/jss.400100403</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| subjects | Animals Artemia electron microscopy Escherichia coli - metabolism Escherichia coli - ultrastructure hybrid ribosome Microscopy, Electron Phenylalanine - metabolism Protein Biosynthesis ribosome structure Ribosomes - metabolism Ribosomes - ultrastructure RNA, Transfer - metabolism |
| title | Structure of functional a salina - E Coli hybrid ribosome by electron microscopy |
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