The ribosome modulates the structural dynamics of the conserved GTPase HflX and triggers tight nucleotide binding

Article ID	Journal	Published Year	Pages	File Type
10804045	Biochimie	2012	13 Pages	PDF

Abstract

âº HflX tightly binds to the 70S ribosome as well as the 50S and 30S subunit. âº Ribosome interaction increases affinity for GTP binding up to 70Â 000-fold. âº HflXÂ·GTP exists in a structurally distinct 50S- and 70S-bound form. âº Only 50S subunit and 70S ribosome induce tight nucleotide binding. âºÂ HflX will mainly exist in the HflXÂ·GTPÂ·ribosome-bound form inÂ vivo.

Keywords

SDS GEF 5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside X-Gal PMSF PEP PAGE MWCO IC50 GDI IPTG 50% inhibitory concentration GTPase Activating Protein Nucleotide binding polyacrylamide gel electrophoresis Fluorescence resonance energy transfer FRET isopropyl-β-d-galactopyranoside equilibrium dissociation constant Stopped-flow P-loop phosphate-binding loop Ribosome sodium dodecyl sulfate GAP elongation factor Initiation factor guanine nucleotide exchange factor phosphoenolpyruvate Phenylmethylsulfonylfluoride Molecular weight cutoff MANT guanine nucleotide dissociation inhibitor pyruvate kinase