Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity.
By B. Shin, David Maag, A. Roll-Mecak, M. Shamsul Arefin, Stephen K. Burley, J. Lorsch, T. Dever, Johns Hopkins. 2002
122 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
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In Immunology
In Molecular Biology
- I. S. Fernández
- Bridget Y. Huang
- A. Hinnebusch
- Sjors H. W. Scheres
- V. Ramakrishnan
- J. Lorsch
- R. Ficner
- B. Kuhle
Citations in the corpus
- Molecular architecture of a eukaryotic translational initiation complex (2013, methodology): “To stabilize eIF5B on the ribosome, we used a mutant defective in GTP hydrolysis (15) in conjunction with GDPCP.”
- Molecular mechanisms of translational control (2004, background): “A second step of GTP hydrolysis on eIF5B is then stimulated by the ribosome, and is required to release eIF5B to render it competent for polypeptide synthesis 13, 14 (FIG.”
- GTP hydrolysis by IF2 guides progression of the ribosome into elongation (2009, result): “This regulatory role of GTP hydrolysis is similar to that observed for eIF5B (Shin et al., 2002).”
- Regulation of translation via mRNA structure in prokaryotes and eukaryotes. (2005, background): “…step controlled by these factors is followed by joining of the 60S subunit, which requires yet another protein factor (Lee et al., 2002; Shin et al., 2002). understanding of the stop-scanning step, we know nothing about the mechanism that actually propels the 40S subunit/ factor…”
- Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, methodology): “Reintroducing the gene in trans from a vector to rescue the severe growth phenotype allows the in vivo testing of eIF5B mutants (42).”
- The scanning mechanism of eukaryotic translation initiation. (2014, background): “Ribosome-stimulated GTP hydrolysis by eIF5B is dispensable for subunit joining (233) but is needed for a functional 80S IC (240– 242) because GTP hydrolysis reduces eIF5B affinity for the 80S IC (233) and triggers its release (242).”
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining (2014, background): “His505 lies only 3.5 Å from H95, explaining why the H505Y mutation results in a reduced affinity for the ribosome and GTPase deficiency in eIF5B (Shin et al, 2002) (see also Supplementary Table S1).”