Elongation factor G with effector loop from elongation factor Tu is inactive in translocation.
Elongation factors Tu and G (EF-Tu and EF-G) alternately interact with the ribosome during the elongation phase of protein biosynthesis. The function of both factors depends on GTP binding, and the factors are ascribed to a superfamily of G-proteins. All G-proteins contain the effector loop, a structural element that is important for the protein's interaction with its target molecule. In this study the effector loop of EF-G was replaced by the loop taken from EF-Tu. The EF-G with EF-Tu loop has markedly decreased GTPase activity and did not catalyze translocation. We conclude that these loops are not functionally interchangeable since the factors interact with different states of the ribosome.
Kolesnikov
Alexander
A
Institute of Protein Research, Russian Academy of Sciences, 142290, Moscow Region, Pushchino, Russia.
Gudkov
Anatoly
A
D000595:Amino Acid Sequence; D001692:Biological Transport; D006160:Guanosine Triphosphate / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D020653:Peptide Elongation Factor G / Q000235:genetics / Q000378:metabolism*; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000235:genetics; D012270:Ribosomes / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000235:genetics / Q000378:metabolism*
D020653:Peptide Elongation Factor G; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu