| dc.contributor.advisor | Stülke, Jörg Prof. Dr. | |
| dc.contributor.author | Mehne, Felix Marco Peter | |
| dc.date.accessioned | 2014-07-14T09:52:32Z | |
| dc.date.available | 2014-07-14T09:52:32Z | |
| dc.date.issued | 2014-07-14 | |
| dc.identifier.uri | http://hdl.handle.net/11858/00-1735-0000-0022-5F16-8 | |
| dc.identifier.uri | http://dx.doi.org/10.53846/goediss-4598 | |
| dc.language.iso | deu | de |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/ | |
| dc.subject.ddc | 570 | de |
| dc.title | Bildung und Homöostase von c-di-AMP in Bacillus subtilis | de |
| dc.type | doctoralThesis | de |
| dc.title.translated | Formation and Homeostasis of c-di-AMP in Bacillus subtilis | de |
| dc.contributor.referee | Walter, Lutz Prof. Dr. | |
| dc.date.examination | 2014-01-15 | |
| dc.description.abstracteng | Signal transduction describes the ability of cells to sense environmental stimuli and transfer this information in order to react appropriately to these stimuli. In this process, signaling nucleotides are often important. These small molecules mediate the cellular communication by regulating a variety of molecular mechanisms. Thus, signal transduction enables cells to adapt to environmental conditions. This work addressed the metabolism of the signaling nucleotide c-di-AMP in the Gram-positive model organism Bacillus subtilis. In B. subtilis, as well as in many Gram-positive pathogens, c-di-AMP is essential. To date, there is no other signaling nucleotide known to be essential. B. subtilis encodes three c-di-AMP synthases: DisA, CdaA and CdaS. CdaA and CdaS were characterized in this work for the first time and based on these insights, new designations were introduced. CdaA is located in the membrane and is encoded together with its regulator CdaR. A functional interaction of these two proteins leads to the activation of CdaA. On the other hand, CdaS is expressed exclusively during sporulation. Thus, CdaS activity is presumably important for sporulation or germination. An N-terminal autoinhibitory domain limits the activity of the catalytic domain. CdaS forms a hexameric complex. While the lack of c-di-AMP is lethal for B. subtilis, overproduction of the nucleotide is also detrimental. This demonstrates that homeostasis of c-di-AMP has to be tightly controlled. High levels of c-di-AMP lead to aberrant curly cell filaments. This phenotype can be suppressed by magnesium ions, which suggests an impact of c-di-AMP on cell wall metabolism. Furthermore, a possible involvement of c-di-AMP in a nitrogen-dependant cell length control was shown. The in vivo detection of a protein complex consisting of CdaA, CdaR and GlmM support the idea that this mechanism may be mediated by a moonlighting activity of GlmM as a sensor of nitrogen supply. The quest for c- di-AMP receptors in B. subtilis in future investigations could identify the key proteins of the participating mechanisms. This would provide a direct correlation of c-di-AMP with the respective cellular functions. | de |
| dc.contributor.coReferee | Kühnel, Karin Dr. | |
| dc.subject.ger | c-di-AMP | de |
| dc.subject.ger | Bacillus subtilis | de |
| dc.subject.ger | zyklisches di-Adenosinmonophosphat | de |
| dc.subject.ger | Diadenylatzyklase | de |
| dc.subject.ger | Signaltransduktion | de |
| dc.subject.eng | c-di-AMP | de |
| dc.subject.eng | Bacillus subtilis | de |
| dc.subject.eng | diadenylate cyclase | de |
| dc.subject.eng | signal transduction | de |
| dc.subject.eng | cyclic di-adenosinemonophosphate | de |
| dc.identifier.urn | urn:nbn:de:gbv:7-11858/00-1735-0000-0022-5F16-8-4 | |
| dc.affiliation.institute | Göttinger Graduiertenschule für Neurowissenschaften, Biophysik und molekulare Biowissenschaften (GGNB) | de |
| dc.subject.gokfull | Biologie (PPN619462639) | de |
| dc.identifier.ppn | 790447967 | |