Cohen, Yaniv. Second messenger-mediated flagellum assembly during the "Caulobacter Crescentus" cell cycle. 2014, Doctoral Thesis, University of Basel, Faculty of Science.
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Official URL: http://edoc.unibas.ch/diss/DissB_11112
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Abstract
The second messenger cyclic-di-guanosine monophosphate (c-di-GMP) is known to control multiple aspects of bacterial growth and development. In C. crescentus, polar developmental such as the synthesis of polar organelles is c-di-GMP dependent. However, the adaptor molecules that sense c-di-GMP and mediate the signal to the appropriate targets are not identified yet.
The main aim goal of this work was to investigate whether and how putative downstream elements are involved in c-di-GMP signalling and to understand their the respectivemechanism of signal transduction mechanisms. Previous results had linked the EAL domain containing protein TipF to flagellar assembly. The focus of this work was the to investigateion of the c-di-GMP signal transduction mechanism involved in TipF activation and the identification of the interfering point ofprocesses of c-di-GMP within the process ofmediated flagellar assembly. Another In an additional projectprotein, we identified the flagellar glycosylation protein FlmA , which was identified as a putative c-di-GMP binding protein in a previous screen. Follow up studies should , was investigated for specificity of c-di-GMP binding specificity of FlmA.
The main aim goal of this work was to investigate whether and how putative downstream elements are involved in c-di-GMP signalling and to understand their the respectivemechanism of signal transduction mechanisms. Previous results had linked the EAL domain containing protein TipF to flagellar assembly. The focus of this work was the to investigateion of the c-di-GMP signal transduction mechanism involved in TipF activation and the identification of the interfering point ofprocesses of c-di-GMP within the process ofmediated flagellar assembly. Another In an additional projectprotein, we identified the flagellar glycosylation protein FlmA , which was identified as a putative c-di-GMP binding protein in a previous screen. Follow up studies should , was investigated for specificity of c-di-GMP binding specificity of FlmA.
Advisors: | Jenal, Urs |
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Committee Members: | Dehio, Christoph |
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Infection Biology > Molecular Microbiology (Jenal) 05 Faculty of Science > Departement Biozentrum > Growth & Development > Molecular Microbiology (Jenal) |
UniBasel Contributors: | Jenal, Urs and Dehio, Christoph |
Item Type: | Thesis |
Thesis Subtype: | Doctoral Thesis |
Thesis no: | 11112 |
Thesis status: | Complete |
Number of Pages: | 153 p. |
Language: | English |
Identification Number: |
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edoc DOI: | |
Last Modified: | 22 Jan 2018 15:52 |
Deposited On: | 12 Feb 2015 13:11 |
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