Title : Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome.

Pub. Date : 2006 Sep 12

PMID : 16940356






4 Functional Relationships(s)
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1 Recently, it was reported that, in contrast to previous observations, the affinity of EF-G was much weaker for GTP than for GDP and that ribosome-catalyzed GDP-GTP exchange would be required for translocation [Zavialov AV, Hauryliuk VV, Ehrenberg M (2005) J Biol 4:9]. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
2 We have reinvestigated GTP/GDP binding and show that EF-G binds GTP and GDP with affinities in the 20 to 40 microM range (37 degrees C), in accordance with earlier reports. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
3 We have reinvestigated GTP/GDP binding and show that EF-G binds GTP and GDP with affinities in the 20 to 40 microM range (37 degrees C), in accordance with earlier reports. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
4 Furthermore, GDP exchange, which is extremely rapid on unbound EF-G, is retarded, rather than accelerated, on the ribosome, which, therefore, is not a nucleotide-exchange factor for EF-G. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens