title: Transiently transfected purine biosynthetic enzymes form stress bodies.
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.
authors: Center for Systems and Synthetic Biology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, United States of America.
authors: Alice
authors: A
authors: Zhao
authors: Mark
authors: M
authors: Tsechansky
authors: Jagannath
authors: J
authors: Swaminathan
authors: Lindsey
authors: L
authors: Cook
authors: Andrew D
authors: AD
authors: Ellington
authors: Edward M
authors: EM
authors: Marcotte
mesh_terms: D053898:Biosynthetic Pathways / Q000502:physiology*; D015153:Blotting, Western; D002384:Catalysis; D003594:Cytoplasmic Granules / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids / Q000235:genetics; D055503:Protein Multimerization; D011687:Purines / Q000096:biosynthesis*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D013312:Stress, Physiological / Q000502:physiology*; D014162:Transfection
chemical_list: D009097:Multienzyme Complexes; D011687:Purines; D011994:Recombinant Proteins; D049452:Green Fluorescent Proteins