Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch
Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the mRNA, required for the formation of the anterior-posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the 3' UTR...
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| Veröffentlicht in: | RNA (Cambridge) 2017-10, Vol.23 (10), p.1552-1568 |
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| creator | Götze, Michael Dufourt, Jérémy Ihling, Christian Rammelt, Christiane Pierson, Stephanie Sambrani, Nagraj Temme, Claudia Sinz, Andrea Simonelig, Martine Wahle, Elmar |
| description | Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the
mRNA, required for the formation of the anterior-posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the
3' UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E, and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of
was confirmed in vivo. Smaug, Cup, and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that "coating" of the RNA by a Me31B•Tral complex may be at the core of repression. |
| doi_str_mv | 10.1261/rna.062208.117 |
| format | Article |
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mRNA, required for the formation of the anterior-posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the
3' UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E, and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of
was confirmed in vivo. Smaug, Cup, and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that "coating" of the RNA by a Me31B•Tral complex may be at the core of repression.</description><identifier>ISSN: 1355-8382</identifier><identifier>EISSN: 1469-9001</identifier><identifier>DOI: 10.1261/rna.062208.117</identifier><identifier>PMID: 28701521</identifier><language>eng</language><publisher>United States: Cold Spring Harbor Laboratory Press</publisher><subject>3' Untranslated regions ; Adenosine triphosphatase ; Animals ; DEAD-box RNA Helicases - genetics ; DEAD-box RNA Helicases - metabolism ; DNA helicase ; Drosophila ; Drosophila melanogaster - embryology ; Drosophila melanogaster - genetics ; Drosophila Proteins - genetics ; Drosophila Proteins - metabolism ; Embryo, Nonmammalian ; Embryogenesis ; Gene Expression Regulation ; Genetics ; Initiation factor eIF-4E ; Insects ; Life Sciences ; mRNA ; Multiprotein Complexes - genetics ; Multiprotein Complexes - metabolism ; Protein Biosynthesis ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; Ribonucleoproteins - genetics ; Ribonucleoproteins - metabolism ; RNA helicase ; RNA Helicases - genetics ; RNA Helicases - metabolism ; RNA, Messenger - chemistry ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism</subject><ispartof>RNA (Cambridge), 2017-10, Vol.23 (10), p.1552-1568</ispartof><rights>2017 Götze et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society.</rights><rights>Copyright Cold Spring Harbor Laboratory Press Oct 2017</rights><rights>Attribution - NonCommercial</rights><rights>2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-a4f4378c53f48ba151ffb7294c4407846f4fbf45f437cf6a49e6ab20afa4e543</citedby><cites>FETCH-LOGICAL-c518t-a4f4378c53f48ba151ffb7294c4407846f4fbf45f437cf6a49e6ab20afa4e543</cites><orcidid>0000-0003-2504-0677 ; 0000-0003-4043-7250</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602113/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602113/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28701521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01595955$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Götze, Michael</creatorcontrib><creatorcontrib>Dufourt, Jérémy</creatorcontrib><creatorcontrib>Ihling, Christian</creatorcontrib><creatorcontrib>Rammelt, Christiane</creatorcontrib><creatorcontrib>Pierson, Stephanie</creatorcontrib><creatorcontrib>Sambrani, Nagraj</creatorcontrib><creatorcontrib>Temme, Claudia</creatorcontrib><creatorcontrib>Sinz, Andrea</creatorcontrib><creatorcontrib>Simonelig, Martine</creatorcontrib><creatorcontrib>Wahle, Elmar</creatorcontrib><title>Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch</title><title>RNA (Cambridge)</title><addtitle>RNA</addtitle><description>Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the
mRNA, required for the formation of the anterior-posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the
3' UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E, and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of
was confirmed in vivo. Smaug, Cup, and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that "coating" of the RNA by a Me31B•Tral complex may be at the core of repression.</description><subject>3' Untranslated regions</subject><subject>Adenosine triphosphatase</subject><subject>Animals</subject><subject>DEAD-box RNA Helicases - genetics</subject><subject>DEAD-box RNA Helicases - metabolism</subject><subject>DNA helicase</subject><subject>Drosophila</subject><subject>Drosophila melanogaster - embryology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila Proteins - genetics</subject><subject>Drosophila Proteins - metabolism</subject><subject>Embryo, Nonmammalian</subject><subject>Embryogenesis</subject><subject>Gene Expression Regulation</subject><subject>Genetics</subject><subject>Initiation factor eIF-4E</subject><subject>Insects</subject><subject>Life Sciences</subject><subject>mRNA</subject><subject>Multiprotein Complexes - genetics</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Protein Biosynthesis</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>Ribonucleoproteins - genetics</subject><subject>Ribonucleoproteins - metabolism</subject><subject>RNA helicase</subject><subject>RNA Helicases - genetics</subject><subject>RNA Helicases - metabolism</subject><subject>RNA, Messenger - chemistry</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><issn>1355-8382</issn><issn>1469-9001</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdUk1vEzEQtRCIlsKVI7LEpRw2ePyx670gpeWjSAEklLvlde2uK8cO9iZSb_x0vEmpoPLB9pv33tgzg9BrIAugLbzPUS9ISymRC4DuCToF3vZNTwg8rWcmRCOZpCfoRSm3FWQ1_BydUNkREBRO0e911rEEPfkUdcDZbrMtpV5wcngaLf6YU0nb0QeNo46p4M3P70vs4z6FvS0HygyMNniji8UXNgSLdbw-wCZV53iDhzv8zTK4OARqSh9sxqOfzPgSPXM6FPvqfj9D68-f1pdXzerHl6-Xy1VjBMip0dxx1kkjmONy0CDAuaGjPTeck07y1nE3OC5mlnGt5r1t9UCJdppbwdkZ-nC03e6Gjb02Nk5ZB7XNfqPznUraq_8j0Y_qJu2VaAkFYNXg3dFgfCS7Wq7UjNWC9nWJPVTu-X2ynH7tbJnUxhdTC6OjTbuioAcpBeFitn37iHqbdrWpoSgKrOO8l6StrMWRZWo3Srbu4QVA1DwHqkrUcQ5UnYMqePPvdx_ofxvP_gCOPa4B</recordid><startdate>20171001</startdate><enddate>20171001</enddate><creator>Götze, Michael</creator><creator>Dufourt, Jérémy</creator><creator>Ihling, Christian</creator><creator>Rammelt, Christiane</creator><creator>Pierson, Stephanie</creator><creator>Sambrani, Nagraj</creator><creator>Temme, Claudia</creator><creator>Sinz, Andrea</creator><creator>Simonelig, Martine</creator><creator>Wahle, Elmar</creator><general>Cold Spring Harbor Laboratory Press</general><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>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-2504-0677</orcidid><orcidid>https://orcid.org/0000-0003-4043-7250</orcidid></search><sort><creationdate>20171001</creationdate><title>Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch</title><author>Götze, Michael ; Dufourt, Jérémy ; Ihling, Christian ; Rammelt, Christiane ; Pierson, Stephanie ; Sambrani, Nagraj ; Temme, Claudia ; Sinz, Andrea ; Simonelig, Martine ; Wahle, Elmar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c518t-a4f4378c53f48ba151ffb7294c4407846f4fbf45f437cf6a49e6ab20afa4e543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>3' Untranslated regions</topic><topic>Adenosine triphosphatase</topic><topic>Animals</topic><topic>DEAD-box RNA Helicases - genetics</topic><topic>DEAD-box RNA Helicases - metabolism</topic><topic>DNA helicase</topic><topic>Drosophila</topic><topic>Drosophila melanogaster - embryology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila Proteins - genetics</topic><topic>Drosophila Proteins - metabolism</topic><topic>Embryo, Nonmammalian</topic><topic>Embryogenesis</topic><topic>Gene Expression Regulation</topic><topic>Genetics</topic><topic>Initiation factor eIF-4E</topic><topic>Insects</topic><topic>Life Sciences</topic><topic>mRNA</topic><topic>Multiprotein Complexes - genetics</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Protein Biosynthesis</topic><topic>Repressor Proteins - genetics</topic><topic>Repressor Proteins - metabolism</topic><topic>Ribonucleoproteins - genetics</topic><topic>Ribonucleoproteins - metabolism</topic><topic>RNA helicase</topic><topic>RNA Helicases - genetics</topic><topic>RNA Helicases - metabolism</topic><topic>RNA, Messenger - chemistry</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Götze, Michael</creatorcontrib><creatorcontrib>Dufourt, Jérémy</creatorcontrib><creatorcontrib>Ihling, Christian</creatorcontrib><creatorcontrib>Rammelt, Christiane</creatorcontrib><creatorcontrib>Pierson, Stephanie</creatorcontrib><creatorcontrib>Sambrani, Nagraj</creatorcontrib><creatorcontrib>Temme, Claudia</creatorcontrib><creatorcontrib>Sinz, Andrea</creatorcontrib><creatorcontrib>Simonelig, Martine</creatorcontrib><creatorcontrib>Wahle, Elmar</creatorcontrib><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>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>RNA (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Götze, Michael</au><au>Dufourt, Jérémy</au><au>Ihling, Christian</au><au>Rammelt, Christiane</au><au>Pierson, Stephanie</au><au>Sambrani, Nagraj</au><au>Temme, Claudia</au><au>Sinz, Andrea</au><au>Simonelig, Martine</au><au>Wahle, Elmar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch</atitle><jtitle>RNA (Cambridge)</jtitle><addtitle>RNA</addtitle><date>2017-10-01</date><risdate>2017</risdate><volume>23</volume><issue>10</issue><spage>1552</spage><epage>1568</epage><pages>1552-1568</pages><issn>1355-8382</issn><eissn>1469-9001</eissn><abstract>Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the
mRNA, required for the formation of the anterior-posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the
3' UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E, and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of
was confirmed in vivo. Smaug, Cup, and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that "coating" of the RNA by a Me31B•Tral complex may be at the core of repression.</abstract><cop>United States</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>28701521</pmid><doi>10.1261/rna.062208.117</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0003-2504-0677</orcidid><orcidid>https://orcid.org/0000-0003-4043-7250</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 3' Untranslated regions Adenosine triphosphatase Animals DEAD-box RNA Helicases - genetics DEAD-box RNA Helicases - metabolism DNA helicase Drosophila Drosophila melanogaster - embryology Drosophila melanogaster - genetics Drosophila Proteins - genetics Drosophila Proteins - metabolism Embryo, Nonmammalian Embryogenesis Gene Expression Regulation Genetics Initiation factor eIF-4E Insects Life Sciences mRNA Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Protein Biosynthesis Repressor Proteins - genetics Repressor Proteins - metabolism Ribonucleoproteins - genetics Ribonucleoproteins - metabolism RNA helicase RNA Helicases - genetics RNA Helicases - metabolism RNA, Messenger - chemistry RNA, Messenger - genetics RNA, Messenger - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism |
| title | Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
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