The joining of ribosomal subunits in eukaryotes requires eIF5B

By T. Pestova, I. Lomakin, Joon-Hwa Lee, S. Choi, T. Dever, C. Hellen. 2000

426 citations recorded by the source corpus.

Subfields: Ecology, Endocrinology, Molecular Biology

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In Ecology

1. A. Pisarev
2. V. Pisareva
3. Jennifer A. Doudna
4. Sjors H. W. Scheres
5. C. Fraser

In Endocrinology

1. A. Pisarev
2. V. Pisareva

In Molecular Biology

1. I. S. Fernández
2. Bridget Y. Huang
3. A. Hinnebusch
4. W. Merrick
5. C. Fraser
6. C. Hellen
7. Sjors H. W. Scheres
8. J. Lorsch

Citations in the corpus

• Internal ribosome entry sites in eukaryotic mRNA molecules. (2001, neutral): “Finally, eIF5B (Table 1) mediates joining of a 60S subunit to the 40S subunit, resulting in formation of an 80S ribosome in which initiator tRNA is positioned in the ribosomal P site and that is competent to begin protein synthesis (Pestova et al. 2000).”
• Molecular architecture of a eukaryotic translational initiation complex (2013, background): “However, it is known that eIF5B also accelerates the rate of 60S recruitment (26, 27).”
• eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining (2014, background): “…of the elongation-competent 80S/70S ribosome, which is achieved by the joining of the large 60S/50S ribosomal subunit, catalyzed by the orthologous GTPases eIF5B, aIF5B and IF2 in eukarya, archaea and bacteria, respectively (Gualerzi et al, 2001; Pestova et al, 2000; Roll-Mecak et al, 2001).”
• Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, methodology): “This is catalyzed by another initiation factor, eIF5B (15).”
• Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. (2006, methodology): “…eluted from MonoQ two fractions earlier than complete eIF2. eIF2 with a truncated -subunit was purified in small quantities from HeLa cells using the purification procedure previously described for eIF2 from RRL (Pestova et al. 2000) as a peak eluted from MonoQ slightly earlier than complete eIF2.”
• Translational control by CPEB: a means to the end (2001, background): “cgi?Q=eif2s*%20not%20eif2ak3&ORG=Hs">eIF2 is hydrolysed, the initiation factors are released, and the 60S subunit joins the 40S (for which it requires eIF5B –GT”
• Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. (2002, neutral): “(Pestova et al., 2000).”
• Structural Characterization of the Human Eukaryotic Initiation Factor 3 Protein Complex by Mass Spectrometry*S (2007, background): “The 60 S ribosomal subunit then joins the 40 S initiation complex aided by eIF5B (7).”