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• W2095556138 abstract "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 ribosome-dependent multiple turnover GTPase activity of EF4, which for the full-length protein is very similar to EF-G. Our findings suggest that the last 44 C-terminal amino acids of EF4 form a sub-domain within the C-terminal domain that is important for GTP-dependent function on the ribosome. Additionally, we show that efficient nucleotide hydrolysis by EF4 on the ribosome depends on a conserved histidine (His 81), similar to EF-G and EF-Tu." @default.
• W2095556138 created "2016-06-24" @default.
• W2095556138 creator A5037044234 @default.
• W2095556138 creator A5059215060 @default.
• W2095556138 date "2015-02-25" @default.
• W2095556138 modified "2023-09-27" @default.
• W2095556138 title "Identification of Two Structural Elements Important for Ribosome-Dependent GTPase Activity of Elongation Factor 4 (EF4/LepA)" @default.
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• W2095556138 doi "https://doi.org/10.1038/srep08573" @default.
• W2095556138 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4339808" @default.
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