The role of tetracycline and macromolecular crowding on the function of elongation factor-Tu

The cellular environment affects dynamics of proteins moving from one conformation into another. Aspects of the cellular environment such as availability of ligands, osmolytes, and antibiotics affect proteins. However, the effect of macromolecular crowding remains debated. The translational GTPase EF-Tu undergoes a large conformational change during its delivery of aa-tRNA to the ribosome. Here, we investigated whether the antibiotic tetracycline or the crowded nature of the cell has an affect on the dynamics of EF-Tu. By comparing the rates of nucleotide binding, the GTPase activity of EF-Tu, and the stability of the EF-Tu- GTP -aa-tRNA complex with and without tetracycline, it was concluded that tetracycline did not affect the function of EF-Tu. Macromolecular crowding by the synthetic crowding agents dextran 40 and PEG 4000 was found to influence the dynamics of nucleotide binding in EF-Tu suggesting the dynamics and function of EF-Tu should be studied in a more cellular-like context.

Authors

• Gzyl, Katherine Elizabeth
• University of Lethbridge. Faculty of Arts and Science

• Tetracyclines
• Genetic translation--Research
• G proteins
• Proteins--Synthesis--Inhibitors
• bacterial translation
• elongation factor-Tu
• macromolecular crowding
• nucleotide binding
• small molecule inhibitors

Identifier

hdl:10133/5087

OAI identifier oai:identifier

oai:opus.uleth.ca:10133/5087