Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation
Roquin controls T-cell activity through interactions with mRNAs of stimulatory receptors. Structural and functional elucidation of its RNA-binding domain reveals how it interacts with constitutive decay elements in the 3' UTR of its targets to regulate their expression. Roquin function in T cel...
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| Veröffentlicht in: | Nature structural & molecular biology 2014-08, Vol.21 (8), p.671-678 |
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| creator | Schlundt, Andreas Heinz, Gitta A Janowski, Robert Geerlof, Arie Stehle, Ralf Heissmeyer, Vigo Niessing, Dierk Sattler, Michael |
| description | Roquin controls T-cell activity through interactions with mRNAs of stimulatory receptors. Structural and functional elucidation of its RNA-binding domain reveals how it interacts with constitutive decay elements in the 3' UTR of its targets to regulate their expression.
Roquin function in T cells is essential for the prevention of autoimmune disease. Roquin interacts with the 3′ untranslated regions (UTRs) of co-stimulatory receptors and controls T-cell activation and differentiation. Here we show that the N-terminal ROQ domain from mouse roquin adopts an extended winged-helix (WH) fold, which is sufficient for binding to the constitutive decay element (CDE) in the
Tnf
3′ UTR. The crystal structure of the ROQ domain in complex with a prototypical CDE RNA stem-loop reveals tight recognition of the RNA stem and its triloop. Surprisingly, roquin uses mainly non-sequence-specific contacts to the RNA, thus suggesting a relaxed CDE consensus and implicating a broader spectrum of target mRNAs than previously anticipated. Consistently with this, NMR and binding experiments with CDE-like stem-loops together with cell-based assays confirm roquin-dependent regulation of relaxed CDE consensus motifs in natural 3′ UTRs. |
| doi_str_mv | 10.1038/nsmb.2855 |
| format | Article |
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Roquin function in T cells is essential for the prevention of autoimmune disease. Roquin interacts with the 3′ untranslated regions (UTRs) of co-stimulatory receptors and controls T-cell activation and differentiation. Here we show that the N-terminal ROQ domain from mouse roquin adopts an extended winged-helix (WH) fold, which is sufficient for binding to the constitutive decay element (CDE) in the
Tnf
3′ UTR. The crystal structure of the ROQ domain in complex with a prototypical CDE RNA stem-loop reveals tight recognition of the RNA stem and its triloop. Surprisingly, roquin uses mainly non-sequence-specific contacts to the RNA, thus suggesting a relaxed CDE consensus and implicating a broader spectrum of target mRNAs than previously anticipated. Consistently with this, NMR and binding experiments with CDE-like stem-loops together with cell-based assays confirm roquin-dependent regulation of relaxed CDE consensus motifs in natural 3′ UTRs.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb.2855</identifier><identifier>PMID: 25026077</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/250 ; 631/45/500 ; 631/535/1266 ; 631/535/878/1263 ; Amino Acid Substitution ; Animals ; Autoimmune diseases ; Base Pairing ; Base Sequence ; Binding Sites ; Biochemistry ; Biological Microscopy ; Cells ; Cellular proteins ; Consensus Sequence ; Crystallography, X-Ray ; Decay ; Genes ; Genetic aspects ; Genetic regulation ; Genetic research ; Life Sciences ; Membrane Biology ; Mice ; Models, Molecular ; Mutagenesis, Site-Directed ; Neurons ; Nuclear Magnetic Resonance, Biomolecular ; Prevention ; Properties ; Protein Binding ; Protein Structure ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Ribonucleic acid ; RNA ; RNA Interference ; RNA Stability ; RNA, Messenger - chemistry ; T cells ; Ubiquitin-Protein Ligases - chemistry ; Ubiquitin-Protein Ligases - genetics</subject><ispartof>Nature structural & molecular biology, 2014-08, Vol.21 (8), p.671-678</ispartof><rights>Springer Nature America, Inc. 2014</rights><rights>COPYRIGHT 2014 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Aug 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c548t-fee07f2c93dc4fc16ec2bc276204da1b78c58f4fb74f90aca744b29eca742e203</citedby><cites>FETCH-LOGICAL-c548t-fee07f2c93dc4fc16ec2bc276204da1b78c58f4fb74f90aca744b29eca742e203</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb.2855$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb.2855$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25026077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schlundt, Andreas</creatorcontrib><creatorcontrib>Heinz, Gitta A</creatorcontrib><creatorcontrib>Janowski, Robert</creatorcontrib><creatorcontrib>Geerlof, Arie</creatorcontrib><creatorcontrib>Stehle, Ralf</creatorcontrib><creatorcontrib>Heissmeyer, Vigo</creatorcontrib><creatorcontrib>Niessing, Dierk</creatorcontrib><creatorcontrib>Sattler, Michael</creatorcontrib><title>Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Roquin controls T-cell activity through interactions with mRNAs of stimulatory receptors. Structural and functional elucidation of its RNA-binding domain reveals how it interacts with constitutive decay elements in the 3' UTR of its targets to regulate their expression.
Roquin function in T cells is essential for the prevention of autoimmune disease. Roquin interacts with the 3′ untranslated regions (UTRs) of co-stimulatory receptors and controls T-cell activation and differentiation. Here we show that the N-terminal ROQ domain from mouse roquin adopts an extended winged-helix (WH) fold, which is sufficient for binding to the constitutive decay element (CDE) in the
Tnf
3′ UTR. The crystal structure of the ROQ domain in complex with a prototypical CDE RNA stem-loop reveals tight recognition of the RNA stem and its triloop. Surprisingly, roquin uses mainly non-sequence-specific contacts to the RNA, thus suggesting a relaxed CDE consensus and implicating a broader spectrum of target mRNAs than previously anticipated. Consistently with this, NMR and binding experiments with CDE-like stem-loops together with cell-based assays confirm roquin-dependent regulation of relaxed CDE consensus motifs in natural 3′ UTRs.</description><subject>631/250</subject><subject>631/45/500</subject><subject>631/535/1266</subject><subject>631/535/878/1263</subject><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Autoimmune diseases</subject><subject>Base Pairing</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Cells</subject><subject>Cellular proteins</subject><subject>Consensus Sequence</subject><subject>Crystallography, X-Ray</subject><subject>Decay</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Genetic regulation</subject><subject>Genetic research</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed</subject><subject>Neurons</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Prevention</subject><subject>Properties</subject><subject>Protein Binding</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA Interference</subject><subject>RNA Stability</subject><subject>RNA, Messenger - 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Structural and functional elucidation of its RNA-binding domain reveals how it interacts with constitutive decay elements in the 3' UTR of its targets to regulate their expression.
Roquin function in T cells is essential for the prevention of autoimmune disease. Roquin interacts with the 3′ untranslated regions (UTRs) of co-stimulatory receptors and controls T-cell activation and differentiation. Here we show that the N-terminal ROQ domain from mouse roquin adopts an extended winged-helix (WH) fold, which is sufficient for binding to the constitutive decay element (CDE) in the
Tnf
3′ UTR. The crystal structure of the ROQ domain in complex with a prototypical CDE RNA stem-loop reveals tight recognition of the RNA stem and its triloop. Surprisingly, roquin uses mainly non-sequence-specific contacts to the RNA, thus suggesting a relaxed CDE consensus and implicating a broader spectrum of target mRNAs than previously anticipated. Consistently with this, NMR and binding experiments with CDE-like stem-loops together with cell-based assays confirm roquin-dependent regulation of relaxed CDE consensus motifs in natural 3′ UTRs.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>25026077</pmid><doi>10.1038/nsmb.2855</doi><tpages>8</tpages></addata></record> |
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| subjects | 631/250 631/45/500 631/535/1266 631/535/878/1263 Amino Acid Substitution Animals Autoimmune diseases Base Pairing Base Sequence Binding Sites Biochemistry Biological Microscopy Cells Cellular proteins Consensus Sequence Crystallography, X-Ray Decay Genes Genetic aspects Genetic regulation Genetic research Life Sciences Membrane Biology Mice Models, Molecular Mutagenesis, Site-Directed Neurons Nuclear Magnetic Resonance, Biomolecular Prevention Properties Protein Binding Protein Structure Protein Structure, Secondary Protein Structure, Tertiary Ribonucleic acid RNA RNA Interference RNA Stability RNA, Messenger - chemistry T cells Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics |
| title | Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation |
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