Immediate GTP hydrolysis upon FtsZ polymerization.
To understand the polymerization dynamics of FtsZ, a bacterial cell division protein similar to tubulin, insight is required into the nature of the nucleotide bound to the polymerized protein. In a previous study, we showed that the FtsZ polymers contain mostly GDP. A recent study challenged this result, suggesting that the polymerized FtsZ is in a GTP-bound state. Here, we show that, when radiolabelled [gamma-32P]-GTP is used to polymerize FtsZ, GTP is hydrolysed instantaneously. The FtsZ polymer contains both GDP and the radiolabelled inorganic phosphate.
Scheffers
Dirk-Jan
DJ
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9750 NN Haren, The Netherlands. dirk-jan.scheffers@pathology.ox.ac.uk
Driessen
Arnold J M
AJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001704:Biopolymers / Q000737:chemistry*; D002855:Chromatography, Thin Layer; D003598:Cytoskeletal Proteins; D019281:Dimerization; D006153:Guanosine Diphosphate / Q000032:analysis; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D010710:Phosphates / Q000032:analysis
D001426:Bacterial Proteins; D001704:Biopolymers; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D010710:Phosphates; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate