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http://purl.uniprot.org/citations/21940857http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21940857http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21940857http://www.w3.org/2000/01/rdf-schema#comment"Although many eukaryotic proteins are amino (N)-terminally acetylated, structural mechanisms by which N-terminal acetylation mediates protein interactions are largely unknown. Here, we found that N-terminal acetylation of the E2 enzyme, Ubc12, dictates distinctive E3-dependent ligation of the ubiquitin-like protein Nedd8 to Cul1. Structural, biochemical, biophysical, and genetic analyses revealed how complete burial of Ubc12's N-acetyl-methionine in a hydrophobic pocket in the E3, Dcn1, promotes cullin neddylation. The results suggest that the N-terminal acetyl both directs Ubc12's interactions with Dcn1 and prevents repulsion of a charged N terminus. Our data provide a link between acetylation and ubiquitin-like protein conjugation and define a mechanism for N-terminal acetylation-dependent recognition."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.org/dc/terms/identifier"doi:10.1126/science.1209307"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.org/dc/terms/identifier"doi:10.1126/science.1209307"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Schulman B.A."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Schulman B.A."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Harper J.W."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Harper J.W."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Scott D.C."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Scott D.C."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Bennett E.J."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Bennett E.J."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Monda J.K."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/author"Monda J.K."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/pages"674-678"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/pages"674-678"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/title"N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/title"N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex."xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/volume"334"xsd:string
http://purl.uniprot.org/citations/21940857http://purl.uniprot.org/core/volume"334"xsd:string