Structural and functional characterization of the bacterial translocation inhibitor GE82832
Letizia Brandi1, Sonia Maffioli, Stefano Donadio
1Department of Biosciences & Biotechnology, University of Camerino, Camerino (MC), Italy.
Abstract:
The structure of GE82832, a translocation inhibitor produced by a soil microorganism, is shown to be highly related to that of dityromycin, a bicyclodecadepsipeptide antibiotic discovered long ago whose characterization had never been pursued beyond its structural elucidation. GE82832 and dityromycin were shown to interfere with both aminoacyl-tRNA and mRNA movement and with the Pi release occurring after ribosome- and EF-G-dependent GTP hydrolysis. These findings and the unusual ribosomal localization of GE82832/dityromycin near protein S13 suggest that the mechanism of inhibition entails an interference with the rotation of the 30S subunit "head" which accompanies the ribosome-unlocking step of translocation.
More Related Videos
05:57Live-Cell Fluorescence Microscopy to Investigate Subcellular Protein Localization and Cell Morphology Changes in Bacteria
Published on: November 23, 2019
12:23Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions
Published on: October 13, 2015
Related Concept Videos
Bacterial Translocation and Protein Secretion
Inhibitors of Bacterial Protein Synthesis
Inhibitors of Gram-positive Cell Wall Synthesis
