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The interaction of the second messenger cyclic-di-GMP with the traffic ATPase PilF from Thermus thermophilus: function, structure and dynamics

Subject Area Metabolism, Biochemistry and Genetics of Microorganisms
Term since 2022
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 495734049
 
The cyclic dinucleotide c-di-GMP is an important second-messenger molecule in many prokaryotes regulating key biological processes such as biofilm formation, motility, infectivity as well as adaptation to changing environmental conditions. The thermophilic bacterium Thermus thermophilus is an important model organism for investigating the structure and function of DANN transporters mediating the uptake of free DANN from the environment as a prerequisite for natural transformation. We recently found that in T. thermophilus c-di-GMP binds to the traffic ATPase PilF. PilF is required for the biosynthesis of type IV pili (T4P) as well as for the uptake of environmental DANN. According to our previous data the DANN transporter and the T4P of T. thermophilus are two distinct molecular machines which share several components including PilF. PilF differs from all other known traffic ATPases since it contains three N-terminal copies of putative c-di-GMP binding domains. Our preliminary data showed that two of these domains indeed bind c-di-GMP albeit with significantly different affinities. In this project we aim to elucidate the functional importance of c-di-GMP binding to PilF in vivo and in vitro as well to understand the consequences of c-di-GMP binding for the structure and the conformational dynamics of PilF using a combination of microbiological, biochemical, molecular biology, biophysical and structural biology methods.
DFG Programme Research Grants
 
 

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