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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Novel data on interactions of elongation factor Ts.

Interactions of EF-Ts with EF-Tu at all steps of the elongation cycle were studied by limited trypsinolysis, gel-filtration, analytical centrifugation and fluorescence polarization techniques. It is shown that EF-Ts does not dissociate from EF-Tu after GDP to GTP exchange, but remains bound to the Aa-tRNA.EF-Tu.GTP complex up to GTP hydrolysis stage on the ribosome. The possible role of these interactions is discussed.[1]


  1. Novel data on interactions of elongation factor Ts. Bubunenko, M.G., Kireeva, M.L., Gudkov, A.T. Biochimie (1992) [Pubmed]
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