Polymerization of the bacterial elongation factor for protein synthesis, EF-Tu.
The bacterial elongation factor for protein synthesis, EF-Tu, polymerizes into fibrils at pH 6.0. These fibrils are 0.7 microM in diameter, at least 200 microns in length, and are positively birefringent. Electron microscopic observations of negatively stained images demonstrates that the EF-Tu fibrils consist of bundles of individual filaments, approximately 5nm in diameter, aligned parallel to the long axis of the fibril. Polymerized EF-Tu exchanges nucleotide rapidly and interacts with the other elongation factor, EF-Ts. The antibiotic kirromycin induces the polymerization of EF-Tu into fibrils and even larger structures under nonpolymerizing conditions.
D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D007700:Kinetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D010445:Peptide Elongation Factors; D011485:Protein Binding; D011487:Protein Conformation; D014357:Trypsin
D046911:Macromolecular Substances; D010445:Peptide Elongation Factors; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D014357:Trypsin