| Grant number: | 24/05454-4 |
| Support Opportunities: | Scholarships in Brazil - Scientific Initiation |
| Start date: | July 01, 2024 |
| End date: | December 31, 2024 |
| Field of knowledge: | Biological Sciences - Microbiology - Biology and Physiology of Microorganisms |
| Principal Investigator: | Robson Francisco de Souza |
| Grantee: | Eduardo Pereira Soares |
| Host Institution: | Instituto de Ciências Biomédicas (ICB). Universidade de São Paulo (USP). São Paulo , SP, Brazil |
Abstract Recently, it has been demonstrated that the fusion of the AMT domain with cytoplasmic domains, endowed with histidine-kinase activity, resulted in the loss of its transporter function, transforming into a specific sensor for external levels of ammonia/ammonium. This process plays a crucial role in nitrogen fixation conducted by microorganisms, proving essential in biogeochemical cycles and ecosystem sustainability. However, the impact of this novel receptor on the regulation of ammonium metabolism has not yet been described. Herein, our objective is to explore the diversity in the composition of proteins within the AMT/Mep/Rh superfamily. We aim to understand how the evolution of the fusion of these transporters with other domains has influenced the uptake and perception of ammonia/ammonium, while also investigating the evolution rates of the fused proteins. This aspect will be addressed through the combination of comparative genome analysis and the use of molecular dynamics simulations. We will systematically identify fusions of AMT domains with signal transduction proteins, mapping their evolutionary trajectory on the phylogenetic tree of AMTs. This approach will enable the classification of fused AMTs, inferring the evolution of the conversion of transporters into transceptors (sensors). Finally, through molecular dynamics simulations, we will assess the ability of representative fused members to act as transporters. | |
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