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Dion, Michael

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Dion, Michael

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2013 - 20152

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Author's Publications: search.filters.isAuthorOfPublication.11917db1-7108-4eab-8bce-8dd35877396e

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    Quantifying Condition-Dependent Intracellular Protein Levels Enables High-Precision Fitness Estimates
    (Public Library of Science, 2013) Geiler-Samerotte, Kerry A.; Hashimoto, Tatsunori; Dion, Michael; Budnik, Bogdan; Airoldi, Edoardo; Drummond, D. Allan
    Countless studies monitor the growth rate of microbial populations as a measure of fitness. However, an enormous gap separates growth-rate differences measurable in the laboratory from those that natural selection can distinguish efficiently. Taking advantage of the recent discovery that transcript and protein levels in budding yeast closely track growth rate, we explore the possibility that growth rate can be more sensitively inferred by monitoring the proteomic response to growth, rather than growth itself. We find a set of proteins whose levels, in aggregate, enable prediction of growth rate to a higher precision than direct measurements. However, we find little overlap between these proteins and those that closely track growth rate in other studies. These results suggest that, in yeast, the pathways that set the pace of cell division can differ depending on the growth-altering stimulus. Still, with proper validation, protein measurements can provide high-precision growth estimates that allow extension of phenotypic growth-based assays closer to the limits of evolutionary selection.
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    Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress
    (Elsevier BV, 2015) Wallace, Edward W.J.; Kear-Scott, Jamie L.; Pilipenko, Evgeny V.; Schwartz, Michael H.; Laskowski, Pawel R.; Rojek, Alexandra E.; Katanski, Christopher D.; Riback, Joshua A.; Dion, Michael; Franks, Alexander M.; Airoldi, Edoardo; Pan, Tao; Budnik, Bogdan; Drummond, D. Allan
    Heat causes protein misfolding and aggregation, and in eukaryotic cells triggers aggregation of proteins and RNA into stress granules. We have carried out extensive proteomic studies to quantify heat-triggered aggregation and subsequent disaggregation in budding yeast, identifying more than 170 endogenous proteins aggregating within minutes of heat shock in multiple subcellular compartments. We demonstrate that these aggregated proteins are not misfolded and destined for degradation. Stable-isotope labeling reveals that even severely aggregated endogenous proteins are disaggregated without degradation during recovery from shock, contrasting with the rapid degradation observed for exogenous thermolabile proteins. Although aggregation likely inactivates many cellular proteins, in the case of a heterotrimeric aminoacyl-tRNA synthetase complex, the aggregated proteins remain active with unaltered fidelity. We propose that most heat-induced aggregation of mature proteins reflects the operation of an adaptive, autoregulatory process of functionally significant aggregate assembly and disassembly that aids cellular adaptation to thermal stress.