http://www.bibsonomy.org/burst/user/mikromolbio/Rhodobacter_capsulatusBibSonomy BuRST Feed for /user/mikromolbio/Rhodobacter_capsulatus2008-09-07T19:52:00+02:00http://www.bibsonomy.org/bibtex/2192438d916f82e78d51d7cfdd8031f65/mikromolbiomikromolbio2008-05-07T15:52:44+02:00Gene_Expression_Regulation Electrophoretic_Mobility_Shift_Assay Deoxyribonuclease_I Luciferases Electrophoresis Polyacrylamide_Gel Rhodobacter_capsulatus Protein_Binding Northern Trans-Activators IFZ Two-Hybrid_System_Techniques Bacterial_Proteins Blotting Oxidation-Reduction Bacterial <span style="color:#555555;">Jutta <a href="http://www.bibsonomy.org/author/Gregor">Gregor</a> und Tanja <a href="http://www.bibsonomy.org/author/Zeller">Zeller</a> und Angelika <a href="http://www.bibsonomy.org/author/Balzer">Balzer</a> und Kerstin <a href="http://www.bibsonomy.org/author/Haberzettl">Haberzettl</a> und Gabriele <a href="http://www.bibsonomy.org/author/Klug">Klug</a> </span><em>Journal of molecular microbiology and biotechnology</em>(<em>2007</em>) <em>PMID: 17693720 . </em>Wed May 07 15:52:44 CEST 2008Journal of molecular microbiology and biotechnologyPMID: 17693720126-39Bacterial regulatory networks include direct contact of response regulator proteins: interaction of RegA and NtrX in Rhodobacter capsulatus132007Gene_Expression_Regulation Electrophoretic_Mobility_Shift_Assay Deoxyribonuclease_I Luciferases Electrophoresis Polyacrylamide_Gel Rhodobacter_capsulatus Protein_Binding Northern Trans-Activators IFZ Two-Hybrid_System_Techniques Bacterial_Proteins Blotting Oxidation-Reduction Bacterial The formation of photosynthetic complexes in facultatively photosynthetic bacteria is controlled by the oxygen tension in the environment. In Rhodobacter capsulatus the two-component system RegB/RegA plays a major role in the redox control of photosynthesis genes but also controls other redox-dependent systems. The response regulator RegA is phosphorylated under low oxygen tension and activates the puf and puc operons, which encode pigment binding proteins, by binding to their promoter regions. Data from a yeast two-hybrid analysis as well as an in vitroanalysis indicate that RegA interacts with the NtrX protein, the response regulator of the NtrY/NtrX two-component system which is believed to be involved in regulation of nitrogen fixation genes. Our further analysis revealed that NtrX is indeed involved in the regulation of the puf and puc operons. Furthermore, we showed that an altered NtrX protein, which is predicted to adopt the conformation of phosphorylated NtrX protein, binds within the puf promoter region close to the RegA binding sites. We conclude that a direct interaction of two response regulators connects the regulatory systems for redox control and nitrogen control.http://www.bibsonomy.org/bibtex/2d09486188bc04d8a07c7ef5a470fbac6/mikromolbiomikromolbio2008-05-07T15:52:44+02:00Gene_Expression_Regulation Escherichia_coli Rhodobacter_capsulatus Oxygen Rhodobacter_sphaeroides Paracoccus_denitrificans Photosynthesis Bacterial_Proteins Light Signal_Transduction Oxidation-Reduction Microbial Bacterial DNA-Binding_Proteins Trans-Activators Repressor_Proteins Photoreceptors Flavoproteins IFZ <span style="color:#555555;">Andreas <a href="http://www.bibsonomy.org/author/Jäger">J&#228;ger</a> und Stephan <a href="http://www.bibsonomy.org/author/Braatsch">Braatsch</a> und Kerstin <a href="http://www.bibsonomy.org/author/Haberzettl">Haberzettl</a> und Sebastian <a href="http://www.bibsonomy.org/author/Metz">Metz</a> und Lisa <a href="http://www.bibsonomy.org/author/Osterloh">Osterloh</a> und Yuchen <a href="http://www.bibsonomy.org/author/Han">Han</a> und Gabriele <a href="http://www.bibsonomy.org/author/Klug">Klug</a> </span><em>Journal of bacteriology</em><em>March2007. </em><em>PMID: 17209035 . </em>Wed May 07 15:52:44 CEST 2008Journal of bacteriologyMarchPMID: 172090352274-82The AppA and PpsR proteins from Rhodobacter sphaeroides can establish a redox-dependent signal chain but fail to transmit blue-light signals in other bacteria1892007Gene_Expression_Regulation Escherichia_coli Rhodobacter_capsulatus Oxygen Rhodobacter_sphaeroides Paracoccus_denitrificans Photosynthesis Bacterial_Proteins Light Signal_Transduction Oxidation-Reduction Microbial Bacterial DNA-Binding_Proteins Trans-Activators Repressor_Proteins Photoreceptors Flavoproteins IFZ The AppA protein of Rhodobacter sphaeroides has the unique ability to sense and transmit redox and light signals. In response to decreasing oxygen tension, AppA antagonizes the transcriptional regulator PpsR, which represses the expression of photosynthesis genes, including the puc operon. This mechanism, which is based on direct protein-protein interaction, is prevented by blue-light absorption of the BLUF domain located in the N-terminal part of AppA. In order to test whether AppA and PpsR are sufficient to transmit redox and light signals, we expressed these proteins in three different bacterial species and monitored oxygen- and blue-light-dependent puc expression either directly or by using a luciferase-based reporter construct. The AppA/PpsR system could mediate redox-dependent gene expression in the alphaproteobacteria Rhodobacter capsulatus and Paracoccus denitrificans but not in the gammaproteobacterium Escherichia coli. Analysis of a prrA mutant strain of R. sphaeroides strongly suggests that light-dependent gene expression requires a balanced interplay of the AppA/PpsR system with the PrrA response regulator. Therefore, the AppA/PpsR system was unable to establish light signaling in other bacteria. Based on our data, we present a model for the interdependence of AppA/PpsR signaling and the PrrA transcriptional activator.