| http://purl.uniprot.org/citations/22124017 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22124017 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22124017 | http://www.w3.org/2000/01/rdf-schema#comment | "RNase R is a processive exoribonuclease that plays an important role in degradation of structured RNAs in Escherichia coli. RNase R is unstable in exponential phase cells; however, under certain stress conditions, RNase R levels increase dramatically due to its stabilization. Binding of tmRNA and SmpB to the C-terminal region of RNase R is required for its instability, and this binding is regulated by acetylation of a single residue, Lys544, in exponential phase cells. RNase R is not acetylated in stationary phase. We show here that only exponential phase RNase R is acetylated because the modifying enzyme, protein lysine acetyltransferase, Pka (YfiQ), is absent from late exponential and stationary phase cells. As a consequence, newly synthesized RNase R remains unmodified. Together with the turnover of preexisting acetylated RNase R, no modified RNase R remains in stationary phase. We find that RNase R in cold-shocked cells also lacks the acetyl modification due to the absence of Pka. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.org/dc/terms/identifier | "doi:10.1261/rna.030213.111"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.org/dc/terms/identifier | "doi:10.1261/rna.030213.111"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/author | "Liang W."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/author | "Liang W."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/author | "Deutscher M.P."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/author | "Deutscher M.P."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/name | "RNA"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/name | "RNA"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/pages | "37-41"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/pages | "37-41"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/title | "Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/title | "Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ)."xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/volume | "18"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://purl.uniprot.org/core/volume | "18"xsd:string |
| http://purl.uniprot.org/citations/22124017 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22124017 |
| http://purl.uniprot.org/citations/22124017 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22124017 |
| http://purl.uniprot.org/citations/22124017 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22124017 |
| http://purl.uniprot.org/citations/22124017 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22124017 |
| http://purl.uniprot.org/uniprot/P21499 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22124017 |
| http://purl.uniprot.org/uniprot/P76594 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22124017 |