Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit
Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis – aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimension...
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| Veröffentlicht in: | FEBS letters 2005-11, Vol.579 (27), p.6049-6054 |
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| container_title | FEBS letters |
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| creator | Jiang, Shoulei Wolfe, Cindy L. Warrington, J. Anthony Norcum, Mona Trempe |
| description | Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis – aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimensional structure of the particle as calculated from electron microscopic images of negatively stained samples of the human ValRS/EF-1H complex. The ca. 12
×
8
nm particle has two distinct domains and each appears to have twofold symmetry. Bound antibodies place two δ subunits near the particle’s center. These data support a dimeric head-to-head arrangement of particle components. |
| doi_str_mv | 10.1016/j.febslet.2005.09.062 |
| format | Article |
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nm particle has two distinct domains and each appears to have twofold symmetry. Bound antibodies place two δ subunits near the particle’s center. These data support a dimeric head-to-head arrangement of particle components.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2005.09.062</identifier><identifier>PMID: 16229838</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>aa-tRNA ; aaRS ; aminoacyl-tRNA ; Aminoacyl-tRNA synthetase ; Antibody ; EF-1H ; Elongation factor 1 ; four subunit form of elongation factor 1 ; Humans ; Multiprotein complex ; Peptide Elongation Factors - chemistry ; Protein biosynthesis ; Protein Conformation ; Protein Subunits - chemistry ; Three-dimensional reconstruction ; Valine-tRNA Ligase - chemistry ; ValRS ; valyl-tRNA synthetase</subject><ispartof>FEBS letters, 2005-11, Vol.579 (27), p.6049-6054</ispartof><rights>2005 Federation of European Biochemical Societies</rights><rights>FEBS Letters 579 (2005) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5064-31f795b7dd23913a09642e2324675de11bf4eef1ed205c528e0245f657b49703</citedby><cites>FETCH-LOGICAL-c5064-31f795b7dd23913a09642e2324675de11bf4eef1ed205c528e0245f657b49703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2005.09.062$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2005.09.062$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,1412,1428,3537,27905,27906,45555,45556,45976,46390,46814</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16229838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jiang, Shoulei</creatorcontrib><creatorcontrib>Wolfe, Cindy L.</creatorcontrib><creatorcontrib>Warrington, J. Anthony</creatorcontrib><creatorcontrib>Norcum, Mona Trempe</creatorcontrib><title>Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis – aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimensional structure of the particle as calculated from electron microscopic images of negatively stained samples of the human ValRS/EF-1H complex. The ca. 12
×
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nm particle has two distinct domains and each appears to have twofold symmetry. Bound antibodies place two δ subunits near the particle’s center. These data support a dimeric head-to-head arrangement of particle components.</description><subject>aa-tRNA</subject><subject>aaRS</subject><subject>aminoacyl-tRNA</subject><subject>Aminoacyl-tRNA synthetase</subject><subject>Antibody</subject><subject>EF-1H</subject><subject>Elongation factor 1</subject><subject>four subunit form of elongation factor 1</subject><subject>Humans</subject><subject>Multiprotein complex</subject><subject>Peptide Elongation Factors - chemistry</subject><subject>Protein biosynthesis</subject><subject>Protein Conformation</subject><subject>Protein Subunits - chemistry</subject><subject>Three-dimensional reconstruction</subject><subject>Valine-tRNA Ligase - chemistry</subject><subject>ValRS</subject><subject>valyl-tRNA synthetase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc9u1DAQhy0EotvCI4By4pbU_x2fUKnaLlIFEuzdcpwJ9cqJl9hpWSTeiufgmUjYleBWTiOPvvnNyB9CrwiuCCbyfFt10KQAuaIYiwrrCkv6BK1IrVjJuKyfohXGhJdCaXaCTlPa4vldE_0cnRBJqa5ZvUI_NncjQNn6Hobk42BDMYKLQ8rj5PLcKGJX5Dso7m3YhzJ_-nBRpP0wd7JNcA4hDl_sH66zLsexJOvCxX4X4Fthh7YI0dngv9t_o379LNLUTIPPL9CzzoYEL4_1DG2urzaX6_L24837y4vb0gkseclIp7RoVNtSpgmzWEtOgTLKpRItENJ0HKAj0FIsnKA1YMpFJ4VquFaYnaE3h9jdGL9OkLLpfXIQgh0gTsnIWkmGef0oSLQigis-g-IAujGmNEJndqPv7bg3BJvFj9maox-z-DFYm9nPPPf6uGBqemj_Th2FzMD6ADz4APv_SzXXV-_o50X24hoLTEiNlxvfHqJg_tl7D6NJzsPgoPWz4mza6B-59jeMartn</recordid><startdate>20051107</startdate><enddate>20051107</enddate><creator>Jiang, Shoulei</creator><creator>Wolfe, Cindy L.</creator><creator>Warrington, J. 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Anthony ; Norcum, Mona Trempe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5064-31f795b7dd23913a09642e2324675de11bf4eef1ed205c528e0245f657b49703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>aa-tRNA</topic><topic>aaRS</topic><topic>aminoacyl-tRNA</topic><topic>Aminoacyl-tRNA synthetase</topic><topic>Antibody</topic><topic>EF-1H</topic><topic>Elongation factor 1</topic><topic>four subunit form of elongation factor 1</topic><topic>Humans</topic><topic>Multiprotein complex</topic><topic>Peptide Elongation Factors - chemistry</topic><topic>Protein biosynthesis</topic><topic>Protein Conformation</topic><topic>Protein Subunits - chemistry</topic><topic>Three-dimensional reconstruction</topic><topic>Valine-tRNA Ligase - chemistry</topic><topic>ValRS</topic><topic>valyl-tRNA synthetase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiang, Shoulei</creatorcontrib><creatorcontrib>Wolfe, Cindy L.</creatorcontrib><creatorcontrib>Warrington, J. 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Anthony</au><au>Norcum, Mona Trempe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2005-11-07</date><risdate>2005</risdate><volume>579</volume><issue>27</issue><spage>6049</spage><epage>6054</epage><pages>6049-6054</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis – aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimensional structure of the particle as calculated from electron microscopic images of negatively stained samples of the human ValRS/EF-1H complex. The ca. 12
×
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nm particle has two distinct domains and each appears to have twofold symmetry. Bound antibodies place two δ subunits near the particle’s center. These data support a dimeric head-to-head arrangement of particle components.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>16229838</pmid><doi>10.1016/j.febslet.2005.09.062</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 2005-11, Vol.579 (27), p.6049-6054 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | aa-tRNA aaRS aminoacyl-tRNA Aminoacyl-tRNA synthetase Antibody EF-1H Elongation factor 1 four subunit form of elongation factor 1 Humans Multiprotein complex Peptide Elongation Factors - chemistry Protein biosynthesis Protein Conformation Protein Subunits - chemistry Three-dimensional reconstruction Valine-tRNA Ligase - chemistry ValRS valyl-tRNA synthetase |
| title | Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit |
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