| http://purl.uniprot.org/citations/26716769 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26716769 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26716769 | http://www.w3.org/2000/01/rdf-schema#comment | "Reversible lysine acetylation is one of the most important protein posttranslational modifications that plays essential roles in both prokaryotes and eukaryotes. However, only a few lysine deacetylases (KDACs) have been identified in prokaryotes, perhaps in part due to their limited sequence homology. Herein, we developed a 'clip-chip' strategy to enable unbiased, activity-based discovery of novel KDACs in the Escherichia coli proteome. In-depth biochemical characterization confirmed that YcgC is a serine hydrolase involving Ser200 as the catalytic nucleophile for lysine deacetylation and does not use NAD(+) or Zn(2+) like other established KDACs. Further, in vivo characterization demonstrated that YcgC regulates transcription by catalyzing deacetylation of Lys52 and Lys62 of a transcriptional repressor RutR. Importantly, YcgC targets a distinct set of substrates from the only known E. coli KDAC CobB. Analysis of YcgC's bacterial homologs confirmed that they also exhibit KDAC activity. YcgC thus represents a novel family of prokaryotic KDACs."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.05322"xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.05322"xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Cole P.A."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Cole P.A."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Zhu H."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Zhu H."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Chen C.S."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Chen C.S."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Deng J.Y."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Deng J.Y."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Ge F."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Ge F."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Liu C.X."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Liu C.X."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Tao S.C."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Tao S.C."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Ahn Y.H."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Ahn Y.H."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Tu S."xsd:string |
| http://purl.uniprot.org/citations/26716769 | http://purl.uniprot.org/core/author | "Tu S."xsd:string |