Publications by authors named "R Marmorstein"
Article Synopsis
- Phosphatidic acid phosphatase (PAP) is an important enzyme involved in lipid metabolism, converting phosphatidic acid into diacylglycerol, which is vital for synthesizing fats and cell membranes.
- Researchers discovered that the antidepressant sertraline inhibits PAP activity in yeast and human cells, working through a noncompetitive mechanism and showing stronger inhibition than a common PAP inhibitor, propranolol.
- Molecular docking studies indicate that sertraline interacts with non-catalytic parts of the enzyme, and tests in yeast demonstrate that overexpressing PAP can counteract the inhibitory effects of sertraline on yeast growth and lipid content.
Cholesterol is a key sterol whose homeostasis is primarily maintained through bile acid metabolism. Proper bile acid formation is vital for nutrient and fat-soluble vitamin absorption and emulsification of lipids. Synthesis of bile acids occurs through two main pathways, both of which rely on 3β-hydroxy-Δ-C-steroid oxidoreductase (HSD3B7) to begin epimerization of the 3β hydroxyl of cholesterol into its active 3α conformation.
View Article and Find Full Text PDFEngineering substrate channeling in a bifunctional terpene synthase.
Proc Natl Acad Sci U S A
October 2024
Article Synopsis
- Fusicoccadiene synthase (PaFS) is a complex enzyme with two main functions: it synthesizes geranylgeranyl diphosphate (GGPP) from smaller molecules and then converts GGPP into fusicoccadiene, a key precursor for another compound.
- The enzyme's two functional domains (prenyltransferase and cyclase) are connected by a flexible linker, allowing the cyclase domains to randomly interact with the central prenyltransferase core, facilitating efficient substrate channeling.
- Research shows that even without a covalent bond between the domains, the cyclase can effectively channel GGPP for conversion, suggesting that physical proximity and structural flexibility play crucial roles in the enzyme's efficiency.
The HIRA histone chaperone complex is comprised of four protein subunits: HIRA, UBN1, CABIN1, and transiently associated ASF1a. All four subunits have been demonstrated to play a role in the deposition of the histone variant H3.3 onto areas of actively transcribed euchromatin in cells.
View Article and Find Full Text PDFEukaryotic genomes are organized by condensin into 3D chromosomal architectures suitable for chromosomal segregation during mitosis. However, molecular mechanisms underlying the condensin-mediated chromosomal organization remain largely unclear. Here, we investigate the role of newly identified interaction between the Cnd1 condensin and Pmc4 mediator subunits in fission yeast, Schizosaccharomyces pombe.
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