Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa
DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher-order RNA structures. We determined the 2.2 Å resolution structure of the core of the Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an A...
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Veröffentlicht in: | Cell 2006-04, Vol.125 (2), p.287-300 |
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creator | Sengoku, Toru Nureki, Osamu Nakamura, Akira Kobayashi, Satoru Yokoyama, Shigeyuki |
description | DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher-order RNA structures. We determined the 2.2 Å resolution structure of the core of the
Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an ATP analog. The ATP analog intensively interacts with both of the domains, thereby bringing them into the closed form, with many interdomain interactions of conserved residues. The bound RNA is sharply bent, avoiding a clash with a conserved α helix in the N-terminal domain. This “wedge” helix should disrupt base pairs by bending one of the strands when a duplex is bound. Mutational analyses indicated that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix. This mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures. |
doi_str_mv | 10.1016/j.cell.2006.01.054 |
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Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an ATP analog. The ATP analog intensively interacts with both of the domains, thereby bringing them into the closed form, with many interdomain interactions of conserved residues. The bound RNA is sharply bent, avoiding a clash with a conserved α helix in the N-terminal domain. This “wedge” helix should disrupt base pairs by bending one of the strands when a duplex is bound. Mutational analyses indicated that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix. This mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2006.01.054</identifier><identifier>PMID: 16630817</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphate - analogs & derivatives ; Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; DEAD-box RNA Helicases ; DNA Mutational Analysis ; Drosophila ; Drosophila melanogaster - enzymology ; Drosophila Proteins - chemistry ; Drosophila Proteins - genetics ; Drosophila Proteins - metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Denaturation ; Oocytes - cytology ; Oocytes - metabolism ; Protein Binding ; Protein Structure, Tertiary ; RNA - chemistry ; RNA - metabolism ; RNA Helicases - chemistry ; RNA Helicases - genetics ; RNA Helicases - metabolism ; Sequence Alignment</subject><ispartof>Cell, 2006-04, Vol.125 (2), p.287-300</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c495t-62ecf0ffaa23752b08db3429f0276b66b48db4e693434f374b10e3fb0cf4cc423</citedby><cites>FETCH-LOGICAL-c495t-62ecf0ffaa23752b08db3429f0276b66b48db4e693434f374b10e3fb0cf4cc423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cell.2006.01.054$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16630817$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sengoku, Toru</creatorcontrib><creatorcontrib>Nureki, Osamu</creatorcontrib><creatorcontrib>Nakamura, Akira</creatorcontrib><creatorcontrib>Kobayashi, Satoru</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><title>Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa</title><title>Cell</title><addtitle>Cell</addtitle><description>DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher-order RNA structures. We determined the 2.2 Å resolution structure of the core of the
Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an ATP analog. The ATP analog intensively interacts with both of the domains, thereby bringing them into the closed form, with many interdomain interactions of conserved residues. The bound RNA is sharply bent, avoiding a clash with a conserved α helix in the N-terminal domain. This “wedge” helix should disrupt base pairs by bending one of the strands when a duplex is bound. Mutational analyses indicated that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix. This mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures.</description><subject>Adenosine Triphosphate - analogs & derivatives</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Crystallography, X-Ray</subject><subject>DEAD-box RNA Helicases</subject><subject>DNA Mutational Analysis</subject><subject>Drosophila</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila Proteins - chemistry</subject><subject>Drosophila Proteins - genetics</subject><subject>Drosophila Proteins - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Denaturation</subject><subject>Oocytes - cytology</subject><subject>Oocytes - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>RNA - chemistry</subject><subject>RNA - metabolism</subject><subject>RNA Helicases - chemistry</subject><subject>RNA Helicases - genetics</subject><subject>RNA Helicases - metabolism</subject><subject>Sequence Alignment</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EglL4ARbIK3YJY8exE4lNaXkKAeK1tRzHBldpUuwE6N-T0krsYDXS1blXmoPQAYGYAOHH01ibqoopAI-BxJCyDTQgkIuIEUE30QAgp1HGBdtBuyFMASBL03Qb7RDOE8iIGKDrx9Z3uu28qvCpCi5g23j8cDvCz_Wnq0tXv-Jigds3gydno0l02nzhe9-0xtV44pvQzN9cpfCLCmoPbVlVBbO_vkP0fH72NL6Mbu4ursajm0izPG0jTo22YK1SNBEpLSAri4TR3AIVvOC8YH3ADM8TljCbCFYQMIktQFumNaPJEB2tdue-ee9MaOXMhaUJVZumC5KLLMtT4P-CRBDBeMp6kK5A3X8UvLFy7t1M-YUkIJeq5VQue3KpWgKR8FM6XK93xcyUv5W12x44WQGml_HhjJdBO1NrUzpvdCvLxv21_w08ko31</recordid><startdate>20060421</startdate><enddate>20060421</enddate><creator>Sengoku, Toru</creator><creator>Nureki, Osamu</creator><creator>Nakamura, Akira</creator><creator>Kobayashi, Satoru</creator><creator>Yokoyama, Shigeyuki</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7SS</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20060421</creationdate><title>Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa</title><author>Sengoku, Toru ; Nureki, Osamu ; Nakamura, Akira ; Kobayashi, Satoru ; Yokoyama, Shigeyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-62ecf0ffaa23752b08db3429f0276b66b48db4e693434f374b10e3fb0cf4cc423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adenosine Triphosphate - analogs & derivatives</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Crystallography, X-Ray</topic><topic>DEAD-box RNA Helicases</topic><topic>DNA Mutational Analysis</topic><topic>Drosophila</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila Proteins - chemistry</topic><topic>Drosophila Proteins - genetics</topic><topic>Drosophila Proteins - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Denaturation</topic><topic>Oocytes - cytology</topic><topic>Oocytes - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>RNA - chemistry</topic><topic>RNA - metabolism</topic><topic>RNA Helicases - chemistry</topic><topic>RNA Helicases - genetics</topic><topic>RNA Helicases - metabolism</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sengoku, Toru</creatorcontrib><creatorcontrib>Nureki, Osamu</creatorcontrib><creatorcontrib>Nakamura, Akira</creatorcontrib><creatorcontrib>Kobayashi, Satoru</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sengoku, Toru</au><au>Nureki, Osamu</au><au>Nakamura, Akira</au><au>Kobayashi, Satoru</au><au>Yokoyama, Shigeyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2006-04-21</date><risdate>2006</risdate><volume>125</volume><issue>2</issue><spage>287</spage><epage>300</epage><pages>287-300</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher-order RNA structures. We determined the 2.2 Å resolution structure of the core of the
Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an ATP analog. The ATP analog intensively interacts with both of the domains, thereby bringing them into the closed form, with many interdomain interactions of conserved residues. The bound RNA is sharply bent, avoiding a clash with a conserved α helix in the N-terminal domain. This “wedge” helix should disrupt base pairs by bending one of the strands when a duplex is bound. Mutational analyses indicated that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix. This mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16630817</pmid><doi>10.1016/j.cell.2006.01.054</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Amino Acid Sequence Animals Crystallography, X-Ray DEAD-box RNA Helicases DNA Mutational Analysis Drosophila Drosophila melanogaster - enzymology Drosophila Proteins - chemistry Drosophila Proteins - genetics Drosophila Proteins - metabolism Models, Molecular Molecular Sequence Data Nucleic Acid Denaturation Oocytes - cytology Oocytes - metabolism Protein Binding Protein Structure, Tertiary RNA - chemistry RNA - metabolism RNA Helicases - chemistry RNA Helicases - genetics RNA Helicases - metabolism Sequence Alignment |
title | Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa |
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