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http://purl.uniprot.org/citations/24736845http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24736845http://www.w3.org/2000/01/rdf-schema#comment"The RNA-binding proteins of the Nanos family play an essential role in germ cell development and survival in a wide range of metazoan species. They function by suppressing the expression of target mRNAs through the recruitment of effector complexes, which include the CCR4-NOT deadenylase complex. Here, we show that the three human Nanos paralogs (Nanos1-3) interact with the CNOT1 C-terminal domain and determine the structural basis for the specific molecular recognition. Nanos1-3 bind CNOT1 through a short CNOT1-interacting motif (NIM) that is conserved in all vertebrates and some invertebrate species. The crystal structure of the human Nanos1 NIM peptide bound to CNOT1 reveals that the peptide opens a conserved hydrophobic pocket on the CNOT1 surface by inserting conserved aromatic residues. The substitutions of these aromatic residues in the Nanos1-3 NIMs abolish binding to CNOT1 and abrogate the ability of the proteins to repress translation. Our findings provide the structural basis for the recruitment of the CCR4-NOT complex by vertebrate Nanos, indicate that the NIMs are the major determinants of the translational repression mediated by Nanos, and identify the CCR4-NOT complex as the main effector complex for Nanos function."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.org/dc/terms/identifier"doi:10.1101/gad.237289.113"xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/author"Bhandari D."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/author"Izaurralde E."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/author"Weichenrieder O."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/author"Jonas S."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/author"Raisch T."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/name"Genes Dev"xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/pages"888-901"xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/title"Structural basis for the Nanos-mediated recruitment of the CCR4-NOT complex and translational repression."xsd:string
http://purl.uniprot.org/citations/24736845http://purl.uniprot.org/core/volume"28"xsd:string
http://purl.uniprot.org/citations/24736845http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24736845
http://purl.uniprot.org/citations/24736845http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24736845
http://purl.uniprot.org/uniprot/A5YKK6#attribution-84F4B6AE948B9A63AB6AEF0094644A67http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/Q8WY41#attribution-84F4B6AE948B9A63AB6AEF0094644A67http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/P60321#attribution-84F4B6AE948B9A63AB6AEF0094644A67http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/P60323#attribution-84F4B6AE948B9A63AB6AEF0094644A67http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/#_A5YKK6-mappedCitation-24736845http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/#_Q8WY41-mappedCitation-24736845http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/Q8WY41http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24736845
http://purl.uniprot.org/uniprot/A5YKK6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24736845