| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/2000/01/rdf-schema#comment | "ATP-dependent protein degradation is controlled principally by substrate recognition. The AAA+ HslU ATPase is thought to bind protein substrates, denature them, and translocate the unfolded polypeptide into the HslV peptidase. The lack of well-behaved high-affinity substrates for HslUV (ClpYQ) has hampered understanding of the rules and mechanism of substrate engagement. We show that HslUV efficiently degrades Arc repressor, especially at heat-shock temperatures. Degradation depends on sequences near the N terminus of Arc. Fusion protein and peptide-binding experiments demonstrate that this sequence is a degradation tag that binds directly to HslU. Strong binding of this tag to the enzyme requires ATP and Mg(2+). Furthermore, fusion of this sequence to a protein with marked mechanical stability leads to complete degradation. Thus, these experiments demonstrate that HslUV is a powerful protein unfoldase and that initial substrate engagement by the HslU ATPase must occur after ATP binding."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb898"xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb898"xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/author | "Sauer R.T."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/author | "Sauer R.T."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/author | "Baker T.A."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/author | "Baker T.A."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/author | "Burton R.E."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/author | "Burton R.E."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/name | "Nat. Struct. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/name | "Nat. Struct. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/pages | "245-251"xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/pages | "245-251"xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/title | "Nucleotide-dependent substrate recognition by the AAA+ HslUV protease."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/title | "Nucleotide-dependent substrate recognition by the AAA+ HslUV protease."xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15696175 |
| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15696175 |
| http://purl.uniprot.org/citations/15696175 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15696175 |