Identification of two structural elements important for ribosome-dependent GTPase activity of elongation factor 4 (EF4/LepA).

ABSTRACT: The bacterial translational GTPase EF4/LepA is structurally similar to the canonical elongation factor EF-G. While sharing core structural features with other translational GTPases, the function of EF4 remains unknown. Recent structural data locates the unique C-terminal domain (CTD) of EF4 in proximity to the ribosomal peptidyl transferase center (PTC). To investigate the functional role of EF4's CTD we have constructed three C-terminal truncation variants. These variants are fully functional with respect to binding mant-GTP and mant-GDP as determined by rapid kinetics, as well as their intrinsic multiple turnover GTPase activity. Furthermore, they are able to form stable complexes with the 70S ribosome and 50S/30S ribosomal subunits. However, successive removal of the C-terminus impairs

SUBMITTER: De Laurentiis EI 

PROVIDER: S-EPMC4339808 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature