Title : The interaction of elongation factor G with N-acetylphenylalanyl transfer RNA-ribosome complexes.

Pub. Date : 1973 Dec

PMID : 4519646






4 Functional Relationships(s)
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1 The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
2 The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
3 The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
4 The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens