| http://purl.uniprot.org/citations/18957436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18957436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18957436 | http://www.w3.org/2000/01/rdf-schema#comment | "DcuB of Escherichia coli catalyzes C4-dicarboxylate/succinate antiport during growth by fumarate respiration. The expression of genes of fumarate respiration, including the genes for DcuB (dcuB) and fumarate reductase (frdABCD) is transcriptionally activated by C4-dicarboxylates via the DcuS-DcuR two-component system, comprising the sensor kinase DcuS, which contains a periplasmic sensing domain for C4-dicarboxylates. Deletion or inactivation of dcuB caused constitutive expression of DcuS-regulated genes in the absence of C4-dicarboxylates. The effect was specific for DcuB and not observed after inactivation of the homologous DcuA or the more distantly related DcuC transporter. Random and site-directed mutation identified three point mutations (T394I, D398N, and K353A) in DcuB that caused a similar derepression as dcuB deletion, whereas the transport activity of the DcuB mutants was retained. Constitutive expression in the dcuB mutants depended on the presence of a functional DcuS-DcuR two-component system. Mutation of residues E79A, R83A, and R127A of DcuB, on the other hand, inactivated growth by fumarate respiration and transport of [14C]succinate, whereas the expression of dcuB'-'lacZ was not affected. Therefore, the antiporter DcuB is a bifunctional protein and has a regulatory function that is independent from transport, and sites for transport and regulation can be differentiated."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m807856200"xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m807856200"xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Unden G."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Unden G."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Bauer J."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Bauer J."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Ackermann B."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Ackermann B."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Kleefeld A."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Kleefeld A."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Kra Mer J."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/author | "Kra Mer J."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/pages | "265-275"xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/pages | "265-275"xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/title | "The fumarate/succinate antiporter DcuB of Escherichia coli is a bifunctional protein with sites for regulation of DcuS-dependent gene expression."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/title | "The fumarate/succinate antiporter DcuB of Escherichia coli is a bifunctional protein with sites for regulation of DcuS-dependent gene expression."xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/volume | "284"xsd:string |
| http://purl.uniprot.org/citations/18957436 | http://purl.uniprot.org/core/volume | "284"xsd:string |