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Systems biology approach reveals possible evolutionarily conserved moonlighting functions for enolase
Gabriela Prado Paludo1, Karina Rodrigues Lorenzatto2, Diego Bonatto3
1Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
Enolase, a glycolytic enzyme, exhibits moonlighting functions beyond energy metabolism. This study reveals conserved non-glycolytic protein interactions across diverse eukaryotes, highlighting enolase
Area of Science:
- Biochemistry
- Systems Biology
- Evolutionary Biology
Background:
- Glycolytic enzymes like enolase possess moonlighting functions beyond their canonical roles.
- The evolutionary conservation of these non-glycolytic functions across different phyla remains underexplored.
Purpose of the Study:
- To investigate the conservation of enolase's moonlighting functions across diverse eukaryotic organisms.
- To analyze enolase's protein-protein interaction (PPI) networks using systems biology approaches.
Main Methods:
- Construction and analysis of enolase PPI networks for Homo sapiens, Drosophila melanogaster, Caenorhabditis elegans, and Saccharomyces cerevisiae.
- Application of modularity, centrality, and functional enrichment analyses.
- Comparative analysis of network structures and conserved protein clusters.
Main Results:
- Enolase acts as a central node in all generated PPI networks.
- Enolase interacts with proteins involved in glycolysis, energy metabolism, transcription, development, and apoptosis.
- Partial conservation of non-glycolytic protein clusters and key regulatory proteins was observed across species.
Conclusions:
- Enolase exhibits conserved moonlighting functions and protein-protein interactions across a wide range of eukaryotes.
- Systems biology analysis of PPI networks provides evidence for the evolutionary persistence of enolase's diverse biological roles.
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