Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions
Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicas...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2008-07, Vol.105 (28), p.9564-9569 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 9569 |
|---|---|
| container_issue | 28 |
| container_start_page | 9564 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 105 |
| creator | Schütz, Patrick Bumann, Mario Oberholzer, Anselm Erich Bieniossek, Christoph Trachsel, Hans Altmann, Michael Baumann, Ulrich |
| description | Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-Å resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity. |
| doi_str_mv | 10.1073/pnas.0800418105 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1073_pnas_0800418105</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>25463013</jstor_id><sourcerecordid>25463013</sourcerecordid><originalsourceid>FETCH-LOGICAL-c618t-1946427380e1bc2cd4f69434778a41b7ed1dd4743cc6b938ec14e0257e1d6b9d3</originalsourceid><addsrcrecordid>eNqFkkFvEzEQhVcIREPhzAmwOCAu23rWXq_NASmKaKlUgQT0bDne2WYjZ53aXtT8e7xK1AAHuHgkzzdvZvxcFC-BngFt2Pl2MPGMSko5SKD1o2IGVEEpuKKPixmlVVNKXvGT4lmMa0qpqiV9WpyAFFQoxWfFsAi7mIwjMYXRpjEg8R1JKyQ7NDERvLrg83I6L4n1m63D-w9kPpBvX-blCl1vTcScGFLwzmFLljuyDT5hP5SHSPohYTA29X6Iz4snnXERXxziaXFz8enH4nN5_fXyajG_Lq0AmUpQXPCqYZIiLG1lW94JxRlvGmk4LBtsoW15w5m1YqmYRAscaVU3CG2-aNlp8XGvux2XG2wt5gGN09vQb0zYaW96_Wdm6Ff61v_UVVblSmaBdweB4O9GjElv-mjROTOgH6MWikHDa_gvWFFFG-BVBt_-Ba79GIb8CpkBVoNULEPne8gGH2PA7mFkoHpyXE-O66PjueL175se-YPFGXhzAKbKo1ytK6lVLSbi_b8J3Y3OJbxPGX21R9cx-fDAVjUXLC9xbNYZr81t6KO--T6tl78eCE4l-wU59NJc</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201351893</pqid></control><display><type>article</type><title>Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Schütz, Patrick ; Bumann, Mario ; Oberholzer, Anselm Erich ; Bieniossek, Christoph ; Trachsel, Hans ; Altmann, Michael ; Baumann, Ulrich</creator><creatorcontrib>Schütz, Patrick ; Bumann, Mario ; Oberholzer, Anselm Erich ; Bieniossek, Christoph ; Trachsel, Hans ; Altmann, Michael ; Baumann, Ulrich</creatorcontrib><description>Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-Å resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0800418105</identifier><identifier>PMID: 18606994</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adenosine triphosphatases ; Amino acids ; Binding Sites ; Biological Sciences ; Crystal structure ; Crystals ; Drug interactions ; eukaryotic initiation factor 4A ; eukaryotic initiation factor 4G ; Eukaryotic Initiation Factor-4A - chemistry ; Eukaryotic Initiation Factor-4A - metabolism ; Eukaryotic Initiation Factor-4G - chemistry ; Eukaryotic Initiation Factor-4G - metabolism ; Messenger RNA ; Molecular structure ; Mutation ; Peptide initiation factors ; Phenotypes ; Protein Binding ; Protein Structure, Tertiary ; protein-protein interactions ; Proteins ; RNA ; RNA helicases ; RNA Helicases - chemistry ; RNA-protein interactions ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; translation initiation factors ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2008-07, Vol.105 (28), p.9564-9569</ispartof><rights>Copyright 2008 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jul 15, 2008</rights><rights>2008 by The National Academy of Sciences of the USA</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c618t-1946427380e1bc2cd4f69434778a41b7ed1dd4743cc6b938ec14e0257e1d6b9d3</citedby><cites>FETCH-LOGICAL-c618t-1946427380e1bc2cd4f69434778a41b7ed1dd4743cc6b938ec14e0257e1d6b9d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/105/28.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25463013$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25463013$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18606994$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schütz, Patrick</creatorcontrib><creatorcontrib>Bumann, Mario</creatorcontrib><creatorcontrib>Oberholzer, Anselm Erich</creatorcontrib><creatorcontrib>Bieniossek, Christoph</creatorcontrib><creatorcontrib>Trachsel, Hans</creatorcontrib><creatorcontrib>Altmann, Michael</creatorcontrib><creatorcontrib>Baumann, Ulrich</creatorcontrib><title>Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-Å resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity.</description><subject>Adenosine triphosphatases</subject><subject>Amino acids</subject><subject>Binding Sites</subject><subject>Biological Sciences</subject><subject>Crystal structure</subject><subject>Crystals</subject><subject>Drug interactions</subject><subject>eukaryotic initiation factor 4A</subject><subject>eukaryotic initiation factor 4G</subject><subject>Eukaryotic Initiation Factor-4A - chemistry</subject><subject>Eukaryotic Initiation Factor-4A - metabolism</subject><subject>Eukaryotic Initiation Factor-4G - chemistry</subject><subject>Eukaryotic Initiation Factor-4G - metabolism</subject><subject>Messenger RNA</subject><subject>Molecular structure</subject><subject>Mutation</subject><subject>Peptide initiation factors</subject><subject>Phenotypes</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>protein-protein interactions</subject><subject>Proteins</subject><subject>RNA</subject><subject>RNA helicases</subject><subject>RNA Helicases - chemistry</subject><subject>RNA-protein interactions</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>translation initiation factors</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFvEzEQhVcIREPhzAmwOCAu23rWXq_NASmKaKlUgQT0bDne2WYjZ53aXtT8e7xK1AAHuHgkzzdvZvxcFC-BngFt2Pl2MPGMSko5SKD1o2IGVEEpuKKPixmlVVNKXvGT4lmMa0qpqiV9WpyAFFQoxWfFsAi7mIwjMYXRpjEg8R1JKyQ7NDERvLrg83I6L4n1m63D-w9kPpBvX-blCl1vTcScGFLwzmFLljuyDT5hP5SHSPohYTA29X6Iz4snnXERXxziaXFz8enH4nN5_fXyajG_Lq0AmUpQXPCqYZIiLG1lW94JxRlvGmk4LBtsoW15w5m1YqmYRAscaVU3CG2-aNlp8XGvux2XG2wt5gGN09vQb0zYaW96_Wdm6Ff61v_UVVblSmaBdweB4O9GjElv-mjROTOgH6MWikHDa_gvWFFFG-BVBt_-Ba79GIb8CpkBVoNULEPne8gGH2PA7mFkoHpyXE-O66PjueL175se-YPFGXhzAKbKo1ytK6lVLSbi_b8J3Y3OJbxPGX21R9cx-fDAVjUXLC9xbNYZr81t6KO--T6tl78eCE4l-wU59NJc</recordid><startdate>20080715</startdate><enddate>20080715</enddate><creator>Schütz, Patrick</creator><creator>Bumann, Mario</creator><creator>Oberholzer, Anselm Erich</creator><creator>Bieniossek, Christoph</creator><creator>Trachsel, Hans</creator><creator>Altmann, Michael</creator><creator>Baumann, Ulrich</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080715</creationdate><title>Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions</title><author>Schütz, Patrick ; Bumann, Mario ; Oberholzer, Anselm Erich ; Bieniossek, Christoph ; Trachsel, Hans ; Altmann, Michael ; Baumann, Ulrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c618t-1946427380e1bc2cd4f69434778a41b7ed1dd4743cc6b938ec14e0257e1d6b9d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Adenosine triphosphatases</topic><topic>Amino acids</topic><topic>Binding Sites</topic><topic>Biological Sciences</topic><topic>Crystal structure</topic><topic>Crystals</topic><topic>Drug interactions</topic><topic>eukaryotic initiation factor 4A</topic><topic>eukaryotic initiation factor 4G</topic><topic>Eukaryotic Initiation Factor-4A - chemistry</topic><topic>Eukaryotic Initiation Factor-4A - metabolism</topic><topic>Eukaryotic Initiation Factor-4G - chemistry</topic><topic>Eukaryotic Initiation Factor-4G - metabolism</topic><topic>Messenger RNA</topic><topic>Molecular structure</topic><topic>Mutation</topic><topic>Peptide initiation factors</topic><topic>Phenotypes</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>protein-protein interactions</topic><topic>Proteins</topic><topic>RNA</topic><topic>RNA helicases</topic><topic>RNA Helicases - chemistry</topic><topic>RNA-protein interactions</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>translation initiation factors</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schütz, Patrick</creatorcontrib><creatorcontrib>Bumann, Mario</creatorcontrib><creatorcontrib>Oberholzer, Anselm Erich</creatorcontrib><creatorcontrib>Bieniossek, Christoph</creatorcontrib><creatorcontrib>Trachsel, Hans</creatorcontrib><creatorcontrib>Altmann, Michael</creatorcontrib><creatorcontrib>Baumann, Ulrich</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schütz, Patrick</au><au>Bumann, Mario</au><au>Oberholzer, Anselm Erich</au><au>Bieniossek, Christoph</au><au>Trachsel, Hans</au><au>Altmann, Michael</au><au>Baumann, Ulrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2008-07-15</date><risdate>2008</risdate><volume>105</volume><issue>28</issue><spage>9564</spage><epage>9569</epage><pages>9564-9569</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-Å resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>18606994</pmid><doi>10.1073/pnas.0800418105</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2008-07, Vol.105 (28), p.9564-9569 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_crossref_primary_10_1073_pnas_0800418105 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine triphosphatases Amino acids Binding Sites Biological Sciences Crystal structure Crystals Drug interactions eukaryotic initiation factor 4A eukaryotic initiation factor 4G Eukaryotic Initiation Factor-4A - chemistry Eukaryotic Initiation Factor-4A - metabolism Eukaryotic Initiation Factor-4G - chemistry Eukaryotic Initiation Factor-4G - metabolism Messenger RNA Molecular structure Mutation Peptide initiation factors Phenotypes Protein Binding Protein Structure, Tertiary protein-protein interactions Proteins RNA RNA helicases RNA Helicases - chemistry RNA-protein interactions Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism translation initiation factors Yeast Yeasts |
| title | Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T02%3A49%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20structure%20of%20the%20yeast%20eIF4A-eIF4G%20complex:%20An%20RNA-helicase%20controlled%20by%20protein-protein%20interactions&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Sch%C3%BCtz,%20Patrick&rft.date=2008-07-15&rft.volume=105&rft.issue=28&rft.spage=9564&rft.epage=9569&rft.pages=9564-9569&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.0800418105&rft_dat=%3Cjstor_cross%3E25463013%3C/jstor_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201351893&rft_id=info:pmid/18606994&rft_jstor_id=25463013&rfr_iscdi=true |