Maximization of information transmission influences selection of native phosphorelay architectures
Autor: | Baldiri Salvado, Ester Vilaprinyo, Ron Milo, Albert Sorribas, Rui Alves |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
Biological design principles Computer science Design elements and principles Biochemistry General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Mathematical Biology Molecular Biology Selection Selection (genetic algorithm) Information transmission Cellular metabolism Mathematical modelling General Neuroscience fungi Computational Biology General Medicine Maximization Biological information transmission 030104 developmental biology Circuit architecture Medicine Synthetic Biology Bacterial signal transduction General Agricultural and Biological Sciences Biological system 030217 neurology & neurosurgery |
Zdroj: | Repositorio Abierto de la UdL Universitad de Lleida PeerJ, Vol 9, p e11558 (2021) PeerJ |
Popis: | Phosphorelays are signal transduction circuits that sense environmental changes and adjust cellular metabolism. Five different circuit architectures account for 99% of all phosphorelay operons annotated in over 9,000 fully sequenced genomes. Here we asked what biological design principles, if any, could explain selection among those architectures in nature. We began by studying kinetically well characterized phosphorelays (Spo0 of Bacillus subtilis and Sln1 of Saccharomyces cerevisiae). We find that natural circuit architecture maximizes information transmission in both cases. We use mathematical models to compare information transmission among the architectures for a realistic range of concentration and parameter values. Mapping experimentally determined phosphorelay protein concentrations onto that range reveals that the native architecture maximizes information transmission in sixteen out of seventeen analyzed phosphorelays. These results suggest that maximization of information transmission is important in the selection of native phosphorelay architectures, parameter values and protein concentrations. The travel related to this work was funded by the Ministerio de Ciencia y educación del gobierno de España (PRX18/00142 to Rui Alves) and the publication fee was funded by the Project G20010 from Universitat de Lleida. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. |
Databáze: | OpenAIRE |
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