The role of tetracycline and macromolecular crowding on the function of elongation factor-Tu
Date
2017
Authors
Gzyl, Katherine Elizabeth
University of Lethbridge. Faculty of Arts and Science
Journal Title
Journal ISSN
Volume Title
Publisher
Lethbridge, Alta. : Universtiy of Lethbridge, Department of Chemistry and Biochemistry
Abstract
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.
Description
Keywords
Tetracyclines , Genetic translation--Research , G proteins , Proteins--Synthesis--Inhibitors , bacterial translation , elongation factor-Tu , macromolecular crowding , nucleotide binding , small molecule inhibitors