Abstract
It has been hypothesized that components of enzymatic pathways might organize into intracellular assemblies to improve their catalytic efficiency or lead to coordinate regulation. Accordingly, de novo purine biosynthesis enzymes may form a purinosome in the absence of purines, and a punctate intracellular body has been identified as the purinosome. We investigated the mechanism by which human de novo purine biosynthetic enzymes might be organized into purinosomes, especially under differing cellular conditions. Irregardless of the activity of bodies formed by endogenous enzymes, we demonstrate that intracellular bodies formed by transiently transfected, fluorescently tagged human purine biosynthesis proteins are best explained as protein aggregation.
Highlights
Enzymes have previously been found to organize into intracellular assemblies that may improve their catalytic efficiency or lead to coordinate regulation
We point direct comparison with our work or An et al.’s, it still supports our claim that transient transfection or otherwise out of context protein expression may play a role in generating punctate bodies
A consideration of the experiments of An et al revealed that the purine-deficient medium did not merely lack purines, but differed in multiple other ways, as well, from the purine-rich medium, and the resulting cellular stress may have induced the aggregation of the recombinant proteins
Summary
Enzymes have previously been found to organize into intracellular assemblies that may improve their catalytic efficiency or lead to coordinate regulation. The trypanosome glycolytic pathway is organized into a glycosome Many such cellular bodies occur naturally, functioning in degradation or storage (e.g., P bodies [1] or actin bodies [2]). While measuring the localization of green fluorescent protein (GFP)-tagged proteins, we identified a surprisingly large number of punctate bodies that accumulated in yeast cells during nutrient starvation [5]. This led us to further speculate whether such bodies were representative of endogenous, functional assemblies, or accidental or pathological aggregates
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