GTP binding and hydrolysis kinetics of human septin 2

• Published in: The FEBS journal Vol. 273; no. 14; pp. 3248 - 3260
• Main Authors: Huang, Yi‐Wei, Surka, Mark C., Reynaud, Denis, Pace‐Asciak, Cecil, Trimble, William S.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.07.2006
• Subjects: Baculoviridae - genetics; Base Sequence; Binding Sites; casein kinase II; Casein Kinase II - antagonists & inhibitors; Casein Kinase II - metabolism; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Drosophila; Enzymes; GTP; GTPase kinetics; Guanosine Diphosphate - metabolism; Guanosine Triphosphate - metabolism; HeLa Cells; Humans; Hydrolysis; In Vitro Techniques; Kinetics; Magnesium - pharmacology; Mutation; Phosphoric Monoester Hydrolases - chemistry; Phosphoric Monoester Hydrolases - genetics; Phosphoric Monoester Hydrolases - isolation & purification; Phosphoric Monoester Hydrolases - metabolism; Phosphoric Monoester Hydrolases - ultrastructure; Phosphorylation; Protein Binding; Proteins; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Saccharomyces cerevisiae; septins; Serine - metabolism

Septins are a family of conserved proteins that are essential for cytokinesis in a wide range of organisms including fungi, Drosophila and mammals. In budding yeast, where they were first discovered, they are thought to form a filamentous ring at the bridge between the mother and bud cells. What reg...