title: In vivo characterization of the scaffold activity of flotillin on the membrane kinase KinC of Bacillus subtilis.
abstract: Scaffold proteins are ubiquitous chaperones that bind to proteins and facilitate the physical interaction of the components of signal transduction pathways or multi-enzymic complexes. In this study, we used a biochemical approach to dissect the molecular mechanism of a membrane-associated scaffold protein, FloT, a flotillin-homologue protein that is localized in functional membrane microdomains of the bacterium Bacillus subtilis. This study provides unambiguous evidence that FloT physically binds to and interacts with the membrane-bound sensor kinase KinC. This sensor kinase activates biofilm formation in B. subtilis in response to the presence of the self-produced signal surfactin. Furthermore, we have characterized the mechanism by which the interaction of FloT with KinC benefits the activity of KinC. Two separate and synergistic effects constitute this mechanism: first, the scaffold activity of FloT promotes more efficient self-interaction of KinC and facilitates dimerization into its active form. Second, the selective binding of FloT to KinC prevents the occurrence of unspecific aggregation between KinC and other proteins that may generate dead-end intermediates that could titrate the activity of KinC. Flotillin proteins appear to play an important role in prokaryotes in promoting effective binding of signalling proteins with their correct protein partners.
authors: Research Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany.|Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
authors: Johannes
authors: J
authors: Schneider
authors: Research Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany.|Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
authors: Benjamin
authors: B
authors: Mielich-Süss
authors: Research Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany.|Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
authors: Richard
authors: R
authors: Böhme
authors: Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.|National Center for Biotechnology (CNB), Spanish Research Council (CSIC), Madrid 28050, Spain.|Research Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany.
authors: Daniel
authors: D
authors: Lopez
mesh_terms: D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D015870:Gene Expression; D015964:Gene Expression Regulation, Bacterial; D008565:Membrane Proteins / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D066329:Protein Aggregates; D011485:Protein Binding; D055503:Protein Multimerization
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D066329:Protein Aggregates; C106354:flotillins