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Eukaryotic translation initiation factor 5B

IF2, eIF5B
Accurate initiation of translation in eukaryotes is complex and requires many factors, some of which are composed of multiple subunits. The process is simpler in prokaryotes which have only three initiation factors (IF1, IF2, IF3). Two of these factors are conserved in eukaryotes: the homolog of IF1 is eIF1A and the homolog of IF2 is eIF5B. This gene encodes eIF5B. Factors eIF1A and eIF5B interact on the ribosome along with other initiation factors and GTP to position the initiation methionine tRNA on the start codon of the mRNA so that translation initiates accurately. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: IF1, CAN, ACID, Elongation Factor Tu, STEP
Papers on IF2
Sliding of a 43S ribosomal complex from the recognized AUG codon triggered by a delay in eIF2-bound GTP hydrolysis.
New
Dmitriev et al., Moscow, Russia. In Nucleic Acids Res, Jan 2016
Instead, it is eIF5-induced GTP hydrolysis and Pi release that irreversibly trap the 48S complex, and this complex is further stabilized by eIF5B and 60S joining.
Initiation factor 2 stabilizes the ribosome in a semirotated conformation.
New
Ermolenko et al., Rochester, United States. In Proc Natl Acad Sci U S A, Jan 2016
The formation of the semirotated intermediate requires the presence of an aminoacylated initiator, fMet-tRNA(fMet), and IF2 in the GTP-bound state.
Directional transition from initiation to elongation in bacterial translation.
New
Rodnina et al., Göttingen, Germany. In Nucleic Acids Res, Jan 2016
After 50S subunit joining, IF2-dependent reactions take place independent of the presence of IF1 or IF3.
Initiation of mRNA translation in bacteria: structural and dynamic aspects.
Review
New
Pon et al., Italy. In Cell Mol Life Sci, Nov 2015
The process begins with the formation of an unstable 30S pre-initiation complex (30S pre-IC) containing initiation factors (IFs) IF1, IF2 and IF3, the translation initiation region of an mRNA and initiator fMet-tRNA whose codon and anticodon pair in the P-site following a first-order rearrangement of the 30S pre-IC produces a locked 30S initiation complex (30SIC); this is docked by the 50S subunit to form a 70S complex that, following several conformational changes, positional readjustments of its ligands and ejection of the IFs, becomes a 70S initiation complex productive in initiation dipeptide formation.
Genetic dissection of the maize kernel development process via conditional QTL mapping for three developing kernel-related traits in an immortalized F2 population.
New
Tang et al., Zhengzhou, China. In Mol Genet Genomics, Oct 2015
To dissect the genetic basis of maize kernel development process, a conditional quantitative trait locus (QTL) analysis was conducted using an immortalized F2 (IF2) population comprising 243 single crosses at two locations over 2 years.
Roles of helix H69 of 23S rRNA in translation initiation.
New
Fredrick et al., Columbus, United States. In Proc Natl Acad Sci U S A, Oct 2015
In bacteria, this process is kinetically controlled by three initiation factors--IF1, IF2, and IF3.
Distribution and diversity of ribosome binding sites in prokaryotic genomes.
Choudhary et al., Huntsville, United States. In Bmc Genomics, 2014
Three initiation factors (IF1, IF2, and IF3) and some ribosomal proteins mediate the assembly and activation of the translation initiation complex.
Could the eIF2α-Independent Translation Be the Achilles Heel of Cancer?
Review
Holcik, Ottawa, Canada. In Front Oncol, 2014
This mechanism, which appears to be shared by some RNA viruses and Internal Ribosome Entry Site-containing cellular mRNAs and utilizes auxiliary proteins, such as eIF5B, eIF2D, and MCT-1, is responsible for the selective translation of cancer-associated genes and could represent a weak point amenable to specific targeting for the treatment of cancer.
The scanning mechanism of eukaryotic translation initiation.
Review
Impact
Hinnebusch, Bethesda, United States. In Annu Rev Biochem, 2013
A second GTPase, eIF5B, catalyzes the joining of the 60S subunit to produce an 80S initiation complex that is competent for elongation.
Molecular architecture of a eukaryotic translational initiation complex.
Impact
Scheres et al., Cambridge, United Kingdom. In Science, 2013
This step is catalyzed by initiation factor eIF5B.
Proofreading of pre-40S ribosome maturation by a translation initiation factor and 60S subunits.
GeneRIF
Tollervey et al., Edinburgh, United Kingdom. In Nat Struct Mol Biol, 2012
propose that recruitment of 60S subunits promotes GTP hydrolysis by Fun12, leading to structural rearrangements within the pre-40S particle that bring Nob1 and the pre-rRNA cleavage site together
Heterogeneous pathways and timing of factor departure during translation initiation.
Impact
Puglisi et al., Stanford, United States. In Nature, 2012
Here we establish in Escherichia coli, using direct single-molecule tracking, the timing of initiator tRNA, initiation factor 2 (IF2; encoded by infB) and 50S subunit joining during initiation.
A translation-like cycle is a quality control checkpoint for maturing 40S ribosome subunits.
Impact
Karbstein et al., Jupiter, United States. In Cell, 2012
Here we show that maturation involves a translation-like cycle whereby the translation factor eIF5B, a GTPase, promotes joining of large (60S) subunits with pre-40S subunits to give 80S-like complexes, which are subsequently disassembled by the termination factor Rli1, an ATPase.
Poliovirus switches to an eIF2-independent mode of translation during infection.
GeneRIF
Lloyd et al., Houston, United States. In J Virol, 2011
The authors show that the cleavage of initiation factor eIF5B during enteroviral infection, along with the viral internal ribosome entry site, plays a role in mediating viral translation under conditions that are nonpermissive for host cell translation.
Structural integrity of {alpha}-helix H12 in translation initiation factor eIF5B is critical for 80S complex stability.
GeneRIF
Dever et al., Bethesda, United States. In Rna, 2011
helix H12 is not critical for eIF5B binding to the ribosome or for GTP hydrolysis with purified ribosomes; however, the length and rigidity of helix H12 are important for formation of stable 80S ribosomal complexes.
Eukaryotic type translation initiation factor 2: structure-functional aspects.
Review
Garber et al., Moscow, Russia. In Biochemistry (mosc), 2011
Translation initiation factor 2 (IF2) is one of key components of the translation initiation system in living cells.
Translation initiation in Archaea: conserved and domain-specific features.
Review
Londei et al., Roma, Italy. In Biochem Soc Trans, 2011
Among these, the protein termed a/eIF2 (archaeal/eukaryotic IF2) and aIF6 (archaeal IF6) are of special interest, since they appear to play key regulatory roles in the Eukarya.
rRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit.
GeneRIF
Dever et al., Bethesda, United States. In Mol Cell Biol, 2009
A mutation in helix h5 of the 18S rRNA in the 40S ribosomal subunit and intragenic mutations in domain II of eIF5B suppress the toxic effects associated with expression of the eIF5B-H480I GTPase-deficient mutant in yeast.
Structure of the 30S translation initiation complex.
Impact
Klaholz et al., Illkirch-Graffenstaden, France. In Nature, 2008
In bacteria, the correct messenger RNA start site and the reading frame are selected when, with the help of initiation factors IF1, IF2 and IF3, the initiation codon is decoded in the peptidyl site of the 30S ribosomal subunit by the fMet-tRNA(fMet) anticodon.
Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C proteases.
GeneRIF
Hellen et al., New York City, United States. In Virology, 2008
3Cpro-mediated cleavage of eIF5B may thus play an accessory role in the shutoff of translation that occurs in enterovirus-infected cells.
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