HflX is a ubiquitous bacterial GTPase that splits and recycles stressed ribosomes. In addition
to HflX, Listeria monocytogenes contains a second HflX homolog, HflXr. Unlike HflX, HflXr …

To overcome the action of antibiotics, bacteria have evolved a variety of different strategies,
such as drug modification, target mutation, and efflux pumps. Recently, we performed a …

Antibiotic resistance in bacteria is typically conferred by proteins that function as efflux
pumps or enzymes that modify either the drug or the antibiotic target. Here we report an …

During stress conditions such as heat shock and antibiotic exposure, ribosomes stall on
messenger RNAs, leading to inhibition of protein synthesis. To remobilize ribosomes …

HflX is a GTP binding protein of unknown function. Based on the presence of the hflX gene
in hflA operon, HflX was believed to be involved in the lytic-lysogenic decision during phage …

Predicted members of the HflX subfamily of phosphate-binding-loop guanosine
triphosphatases (GTPases) are widely distributed in the bacterial kingdom but remain …

Adverse cellular conditions often lead to nonproductive translational stalling and arrest of
ribosomes on mRNAs. Here, we used fast kinetics and cryo-EM to characterize Escherichia …

HflX GTPases are found in all three domains of life, the Bacteria, Archaea, and Eukarya. HflX
from Escherichia coli has been shown to bind to the 50S ribosomal subunit in a nucleotide …

Using a combination of biochemical, structural probing and rapid kinetics techniques we
reveal for the first time that the universally conserved translational GTPase (trGTPase) HflX …

Mutations in ribosomal proteins L4 and L22 confer resistance to erythromycin and other
macrolide antibiotics in a variety of bacteria. L4 and L22 have elongated loops whose tips …