Prof Julie Maupin; Dept of Microbiology and Cell Science, University of Florida
Prof. Maupin-Furlow is an ASM Academy Fellow, Professor and Graduate Coordinator in the Department of Microbiology and Cell Science at the University of Florida, who leads an internationally recognized research team focused on the metabolism and physiology of archaea including those from extreme environments (extremophiles). She uses a multidisciplinary approach that includes proteomic, biochemical, molecular, genomic, and structural biology techniques to address research questions on how cells respond to and function in extreme environments and what features may be evolutionarily conserved or distinct among this group of organisms. Her work provides a deeper understanding of molecular mechanisms fundamental to cell biology including discoveries in redox biology, post-translational modifications, ubiquitin-proteasomes, sulfur mobilization, as well as primary and secondary metabolism. Maupin-Furlow has also made scientific advances in the use of microorganisms and their enzymes as industrial biocatalysts to generate renewable fuels and chemicals. Patented molecular tools and enzyme biocatalysts derived from extremophilic microorganisms for industrial application are practical outcomes of her program.
The ubiquitin-proteasome system (UPS) is a fundamental regulator of protein homeostasis, yet its evolutionary origins and functional diversity remain incompletely understood. Archaea provide a unique opportunity to address these questions, as they possess streamlined UPS-related pathways that share key features with their eukaryotic counterparts while supporting life under extreme environmental conditions. Our studies of the halophilic archaeon Haloferax volcanii have uncovered an interconnected ubiquitin-like signaling network in which small archaeal modifier proteins (SAMPs), the multifunctional E1-like enzyme UbaA, the rhodanese-domain protein UbaC, and methionine sulfoxide reductase A (MsrA) coordinate protein modification and sulfur mobilization pathways. In addition, lysine acetylation intersects with these ubiquitin-like conjugation systems, revealing extensive crosstalk among post-translational regulatory mechanisms. Current efforts focus on defining how these pathways are integrated to control protein fate, enzyme activity, and sulfur metabolism. These findings reveal unexpected links between proteostasis and sulfur trafficking and provide new insights into the evolution of ubiquitin-like signaling across the domains of life. More broadly, this work highlights how archaeal systems can illuminate fundamental principles of post-translational regulation while providing a foundation for engineering robust extremophilic microorganisms for biotechnology and sustainable biomanufacturing applications.
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