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http://purl.uniprot.org/citations/20355727http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20355727http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20355727http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/20355727http://www.w3.org/2000/01/rdf-schema#comment"A prokaryotic protein tagging system called pupylation that is analogous to ubiquitylation in eukaryotes has recently been described. In this process, prokaryotic ubiquitin-like protein (Pup) is coupled to substrate proteins via an isopeptide bond in order to target them for degradation by the proteasome. The ligation occurs via a condensation reaction involving a carboxylate of the C-terminal glutamate of Pup (located in a conserved terminal Gly-Gly-Glu motif) and the side-chain amino group of a substrate lysine. Here we have used a combination of NMR and biochemical experiments with free lysine and a physiological protein substrate (PanB) to show that the coupling occurs through the side-chain carboxylate of the glutamate in the GGE motif rather than the carboxy terminus but that the glutamate must be located at the C-terminal position to be coupled."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.org/dc/terms/identifier"doi:10.1021/ja910546x"xsd:string
http://purl.uniprot.org/citations/20355727http://purl.org/dc/terms/identifier"doi:10.1021/ja910546x"xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Sutter M."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Sutter M."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Weber-Ban E."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Weber-Ban E."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Allain F.H."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Allain F.H."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Damberger F.F."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Damberger F.F."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Imkamp F."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/author"Imkamp F."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/name"J. Am. Chem. Soc."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/name"J. Am. Chem. Soc."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/pages"5610-5612"xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/pages"5610-5612"xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/title"Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/title"Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate."xsd:string
http://purl.uniprot.org/citations/20355727http://purl.uniprot.org/core/volume"132"xsd:string