Show simple item record Coatham, Mackenzie L. Brandon, Harland E. Fischer, Jeffrey J. Schummer, Tobias Wieden, Hans-Joachim 2017-03-17T22:01:06Z 2017-03-17T22:01:06Z 2016
dc.identifier.citation Coatham, M.L., Brandon, H.E., Fischer, J.J., Schummer, T., & Wieden, H. (2016). The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome. Nucleic Acids Research, 44(4), 1952-1963. doi:10.1093/nar/gkv1524 en_US
dc.description Sherpa Romeo green journal. Permission to archive final published verison en_US
dc.description.abstract 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 binds to the E-site of the 70S ribosome and that its GTPase activity is modulated by peptidyl transferase centre (PTC) and peptide exit tunnel (PET) binding antibiotics, suggesting a previously undescribed mode of action for these antibiotics. Our rapid kinetics studies reveal that HflX functions as a ribosome splitting factor that disassembles the 70S ribosomes into its subunits in a nucleotide dependent manner. Furthermore, our probing and hydrolysis studies show that the ribosome is able to activate trGTPases bound to its E-site. This is, to our knowledge, the first case in which the hydrolytic activity of a translational GTPase is not activated by the GTPase activating centre (GAC) in the ribosomal A-site. Furthermore, we provide evidence that the bound state of the PTC is able to regulate the GTPase activity of E-site bound HflX. en_US
dc.language.iso en_US en_US
dc.publisher Oxford University Press en_US
dc.subject GTPase en_US
dc.subject Guanosine triphosphatase en_US
dc.subject Ribosomes en_US
dc.subject Ribosome en_US
dc.subject E-site en_US
dc.subject Splitting factor en_US
dc.subject Antibiotics en_US
dc.subject HflX en_US
dc.title The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution University of Alberta en_US
dc.publisher.institution University of Lethbridge en_US

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