Objective
The project is directed to the investigation of the translocation step in protein biosynthesis. The main goals of the project are studies of the structure- function relationships of elongation factor G both in isolated state and upon its interaction with the ribosome. The methodological approach will be site-directed mutagenesis of EF-G from E. coli and T. thermophilus. These parallel studies will complement each other.
The primary attention will be focussed on the conformational changes of EF-G that occur during GDP/GTP exchange and GTP-hydrolysis as well as the translocation activity of EF-G. Different mutated forms of EF-G will be constructed by mutagenesis in domains G, IV as well as between domains V and G. The planning of the mutational work will be based on the recently determined tertiary structure of EF-G. The isolated mutants will be studied by crystallography and using functional tests in the cell-free translation systems and by different physico-chemical methods.
The studies will help to understand ribosomal translocation and can also be related to other GTPases. The results will be presented for publication in international journals.
Topic(s)
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211 00 Lund
Sweden