Guanosinetriphosphatase activity dependent on elongation factor Tu and ribosomal protein L7/L12.
Incubation of electrophoretically pure samples of the Escherichia coli 50S ribosomal protein L7/L12 together with elongation factor Tu leads to the hydrolysis of GTP. Addition of elongation factor Ts stimulates this reaction. Elongation factor G cannot replace elongation factor Tu for the ribosome-free GTPase reaction dependent on L7/L12. The data suggest that elongation factor Tu and the protein L7/L12 interact directly at the ribosomal A site.
D001426:Bacterial Proteins / Q000378:metabolism; D004926:Escherichia coli; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism*; D010445:Peptide Elongation Factors; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism
D001426:Bacterial Proteins; D010445:Peptide Elongation Factors; D012333:RNA, Messenger; D012269:Ribosomal Proteins; D012343:RNA, Transfer; D010744:Phosphoric Monoester Hydrolases; D020963:GTP Phosphohydrolase-Linked Elongation Factors