| http://purl.uniprot.org/citations/10383384 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10383384 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10383384 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/10383384 | http://www.w3.org/2000/01/rdf-schema#comment | "The Escherichia coli gene rluA, coding for the pseudouridine synthase RluA that forms 23 S rRNA pseudouridine 746 and tRNA pseudouridine 32, was deleted in strains MG1655 and BL21/DE3. The rluA deletion mutant failed to form either 23 S RNA pseudouridine 746 or tRNA pseudouridine 32. Replacement of rluA in trans on a rescue plasmid restored both pseudouridines. Therefore, RluA is the sole protein responsible for the in vivo formation of 23 S RNA pseudouridine 746 and tRNA pseudouridine 32. Plasmid rescue of both rluA-strains using an rluA gene carrying asparagine or threonine replacements for the highly conserved aspartate 64 demonstrated that neither mutant could form 23 S RNA pseudouridine 746 or tRNA pseudouridine 32 in vivo, showing that this conserved aspartate is essential for enzyme-catalyzed formation of both pseudouridines. In vitro assays using overexpressed wild-type and mutant synthases confirmed that only the wild-type protein was active despite the overexpression of wild-type and mutant synthases in approximately equal amounts. There was no difference in exponential growth rate between wild-type and MG1655(rluA-) either in rich or minimal medium at 24, 37, or 42 degrees C, but when both strains were grown together, a strong selection against the deletion strain was observed."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.27.18880"xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.27.18880"xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.27.18880"xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Niu L."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Niu L."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Conrad J."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Conrad J."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Lane B.G."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Lane B.G."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Raychaudhuri S."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Raychaudhuri S."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Ofengand J."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/author | "Ofengand J."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/pages | "18880-18886"xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/pages | "18880-18886"xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/title | "Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA."xsd:string |
| http://purl.uniprot.org/citations/10383384 | http://purl.uniprot.org/core/title | "Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA."xsd:string |