GTP hydrolysis by IF2 guides progression of the ribosome into elongation
By R. Marshall, Colin Echeverría Aitken, Joseph D. Puglisi. 2009
99 citations recorded by the source corpus.
Summary Recent structural data have revealed two distinct conformations of the ribosome during initiation. We employed single-molecule fluorescence methods to probe the dynamic relation of these ribosomal conformations in real time. In the absence of initiation factors, the ribosome assembles in two distinct conformations. The initiation factors discriminate between these two conformations, guiding assembly of the conformation that can enter the elongation cycle. In particular, IF2 both accelerates the rate of subunit joining and actively promotes the transition to the elongation-competent conformation. Blocking GTP hydrolysis by IF2 results in 70S complexes formed in the conformation unable to enter elongation. We observe that rapid GTP hydrolysis by IF2 drives the transition to the elongation-competent conformation, thus committing the ribosome to enter the elongation cycle.
Subfields: Genetics, Molecular Biology
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In Molecular Biology
Citations in the corpus
- Initiation factor 2 stabilizes the ribosome in a semirotated conformation (2015, background): “Consistent with early proposals (24), GTP hydrolysis likely triggers conformational changes in IF2 that result in the transition of the ribosomal subunits to the nonrotated orientation and the outward movement of the L1 stalk into the open conformation.”
- Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association (2016, result): “This assignment is in overall agreement with single-molecule fluorescence resonance energy transfer data reporting an early 70S-IC in the rotated state that is converted into an elongation-competent 70S complex by back rotation of the 30S subunit (16, 17).”