保守的GTP酶HflX是一种核糖体分裂因子，它与细菌核糖体的E位点结合。
The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome.
作者信息
Coatham Mackenzie L, Brandon Harland E, Fischer Jeffrey J, Schümmer Tobias, Wieden Hans-Joachim
机构信息
Alberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, T1K 3M4, Canada.
Alberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, T1K 3M4, Canada
出版信息
Nucleic Acids Res. 2016 Feb 29;44(4):1952-61. doi: 10.1093/nar/gkv1524. Epub 2016 Jan 4.
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.
通过结合生化、结构探测和快速动力学技术，我们首次揭示了普遍保守的翻译GTP酶（trGTP酶）HflX与70S核糖体的E位点结合，并且其GTP酶活性受到肽基转移酶中心（PTC）和肽出口通道（PET）结合抗生素的调节，这表明这些抗生素存在一种以前未描述的作用模式。我们的快速动力学研究表明，HflX作为一种核糖体分裂因子，以核苷酸依赖的方式将70S核糖体分解为其亚基。此外，我们的探测和水解研究表明，核糖体能够激活与其E位点结合的trGTP酶。据我们所知，这是翻译GTP酶的水解活性未被核糖体A位点的GTP酶激活中心（GAC）激活的首个案例。此外，我们提供的证据表明，PTC的结合状态能够调节E位点结合的HflX的GTP酶活性。
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