Divergent effects of fluoroaluminates on the peptide chain elongation factors EF-Tu and EF-G as members of the GTPase superfamily.
Fluoraluminates are thought to mimic the gamma-phosphate of GTP and thus, together with GDP, perturb the functioning of heterotrimeric GTP-binding G-proteins. Here we show they do inhibit the ribosome-stimulated GTPase activity of EF-G from Escherichia coli via the formation of a stable complex with EF-G-GDP and ribosomes. In contrast, no perturbed interactions were observed in a similar ribosomal complex with EF-Tu. Interestingly, in the absence of ribosomes both EF-Tu an EF-G remain totally unaffected by fluoraluminates. For members of the GTPase superfamily such differential effects have not been described before.
Mesters
J R
JR
Department of Biochemistry, Leiden University, The Netherlands.
Martien de Graaf
J
J
Kraal
B
B
D000433:1-Propanol / Q000494:pharmacology; D000535:Aluminum / Q000494:pharmacology*; D000900:Anti-Bacterial Agents / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D005459:Fluorides / Q000494:pharmacology*; D005461:Fluorine / Q000494:pharmacology*; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu / Q000302:isolation & purification / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000302:isolation & purification / Q000378:metabolism*; D011728:Pyridones / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D011728:Pyridones; C053629:fluoroaluminum; D005461:Fluorine; D000433:1-Propanol; D000535:Aluminum; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D010444:Peptide Elongation Factor Tu; C008536:mocimycin; D005459:Fluorides