Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu.aminoacyl-tRNA complex with temperature.
Recent observations indicate that the stoichiometry for the complex between EF-Tu.GTP and aminoacyl-tRNA (aa-tRNA) changes with temperature. At 37 degrees C two EF-Tu.GTPs bind one aa-tRNA in an extended ternary complex, but at 0 degrees C the complex has 1:1 stoichiometry. However, the present experiments show that there are two GTPs hydrolyzed on EF-Tu per peptide bond in poly(Phe) synthesis at 37 degrees C as well as at 0 degrees C. This indicates two different pathways for the enzymatic binding of aa-tRNA to the A-site on the ribosome.
Dinçbaş
V
V
Department of Molecular Biology, BMC, Uppsala, Sweden.
Bilgin
N
N
Scoble
J
J
Ehrenberg
M
M
D004926:Escherichia coli; D006160:Guanosine Triphosphate / Q000378:metabolism*; D008968:Molecular Conformation; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides; D010649:Phenylalanine / Q000378:metabolism*; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
D010455:Peptides; D012346:RNA, Transfer, Amino Acyl; C012001:polyphenylalanine; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu