gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

TIF5 Tif5p

eIF5, Eukaryotic translation initiation factor 5, TIF5
Eukaryotic translation initiation factor-5 (EIF5) interacts with the 40S initiation complex to promote hydrolysis of bound GTP with concomitant joining of the 60S ribosomal subunit to the 40S initiation complex. The resulting functional 80S ribosomal initiation complex is then active in peptidyl transfer and chain elongations (summary by Si et al., 1996 [PubMed 8663286]).[supplied by OMIM, May 2010] (from NCBI)
Top mentioned proteins: eIF2B, CAN, ACID, 110-kDa, IF2
Papers on eIF5
Sliding of a 43S ribosomal complex from the recognized AUG codon triggered by a delay in eIF2-bound GTP hydrolysis.
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.
Altered machinery of protein synthesis in Alzheimer's: from the nucleolus to the ribosome.
Ferrer et al., l'Hospitalet de Llobregat, Spain. In Brain Pathol, Nov 2015
Several genes encoding ribosomal proteins are abnormally regulated and protein levels of translation initiation factors eIF2α, eIF3η and eIF5, and elongation factor eEF2, are altered in the CA1 region in AD.
Integrated Transcriptional and Proteomic Analysis of Growth Hormone Suppression Mediated by Trichothecene T-2 Toxin in Rat GH3 Cells.
Yuan et al., Wuhan, China. In Toxicol Sci, Oct 2015
Our results showed that trichothecenes suppressed the synthesis of growth hormone 1 (Gh1) and inhibited the eukaryotic transcription and translation initiation by suppressing aminoacyl-tRNA synthetases transcription, inducing eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and reducing eukaryotic translation initiation factor 5 a.
Conformational Differences between Open and Closed States of the Eukaryotic Translation Initiation Complex.
Ramakrishnan et al., Bethesda, United States. In Mol Cell, Sep 2015
Translation initiation in eukaryotes begins with the formation of a pre-initiation complex (PIC) containing the 40S ribosomal subunit, eIF1, eIF1A, eIF3, ternary complex (eIF2-GTP-Met-tRNAi), and eIF5.
Analysis of RNA Interference Lines Identifies New Functions of Maternally-Expressed Genes Involved in Embryonic Patterning in Drosophila melanogaster.
Lasko et al., Montréal, Canada. In G3 (bethesda), Jun 2015
This analysis revealed requirements for ttk, pbl, Hip14, eIF5, eIF4G, and CG9977 for progression through early oogenesis.
microRNA-107 functions as a candidate tumor suppressor gene in renal clear cell carcinoma involving multiple genes.
Zhang et al., Beijing, China. In Urol Oncol, May 2015
In addition, eukaryotic translation initiation factor 5 was found to be a direct target of miR-107 and exhibited an inverse relationship with miR-107.
ABC50 mutants modify translation start codon selection.
Proud et al., Southampton, United Kingdom. In Biochem J, May 2015
It is widely accepted that the presence and movement of eIF1, eIF1A and eIF5 are key factors in modulating the stringency of start-site selection, which normally requires an AUG codon in an appropriate sequence context.
Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2.
Schmitt et al., Palaiseau, France. In Nucleic Acids Res, Apr 2015
In eukaryotes, the GTPase activity of eIF2 is assisted by a GTPase-activating protein (GAP), eIF5.
The scanning mechanism of eukaryotic translation initiation.
Hinnebusch, Bethesda, United States. In Annu Rev Biochem, 2013
Binding of Met-tRNAi to the small (40S) ribosomal subunit, in a ternary complex (TC) with eIF2-GTP, is stimulated by eukaryotic initiation factor 1 (eIF1), eIF1A, eIF3, and eIF5, and the resulting preinitiation complex (PIC) joins the 5' end of mRNA preactivated by eIF4F and poly(A)-binding protein.
A new function and complexity for protein translation initiation factor eIF2B.
Pavitt et al., Manchester, United Kingdom. In Cell Cycle, 2013
Specifically it displaces a third translation factor eIF5 (a dual function GAP and GDI) from eIF2•GDP/eIF5 complexes.
The hsa-miR-5787 represses cellular growth by targeting eukaryotic translation initiation factor 5 (eIF5) in fibroblasts.
Kim et al., South Korea. In Biochem Biophys Res Commun, 2012
miR-5787 represses cell growth, in part, by targeting eIF5.
Eukaryotic type translation initiation factor 2: structure-functional aspects.
Garber et al., Moscow, Russia. In Biochemistry (mosc), 2011
There are also new data on initiation factors eIF5 and eIF2B that directly interact with eIF2 and control its participation in nucleotide exchange.
eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation.
Pavitt et al., Manchester, United Kingdom. In Nature, 2010
eIF5 functions in start site selection as a GTPase accelerating protein (GAP) for the eIF2.GTP.tRNA(i)(Met)
IRES-induced conformational changes in the ribosome and the mechanism of translation initiation by internal ribosomal entry.
Hellen, New York City, United States. In Biochim Biophys Acta, 2009
type 3 IRESs (epitomized by Hepatitis C virus) binds independently to eukaryotic initiation factor (eIF) 3, and to the solvent-accessible surface and E-site of the 40S subunit: addition of eIF2-GTP/initiator tRNA is sufficient to form a 48S complex that can join a 60S subunit in an eIF5/eIF5B-mediated reaction to form an active ribosome.
Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiation.
Pavitt et al., Manchester, United Kingdom. In Biochem Soc Trans, 2008
A complex example of this system is seen in eukaryotic translation initiation between eIF (eukaryotic initiation factor) 2, a G-protein, its five-subunit GEF, eIF2B, and its GAP, eIF5.
Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection.
Asano et al., Boston, United States. In J Biol Chem, 2008
The direct interaction at eIF1 places eIF5 near the decoding site of the 40 S subunit.
Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex.
McCarthy et al., Oxford, United Kingdom. In Proc Natl Acad Sci U S A, 2007
eIF-5 can form the multifactor complex with the ribosome 40S subunit.
An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation.
Asano et al., Manhattan, United States. In Embo J, 2006
The eIF2/eIF5 complex represents a cytoplasmic reservoir for eIF2 that antagonizes eIF2B-promoted guanine nucleotide exchange, enabling coordinated regulation of translation initiation.
The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5.
Baumann et al., Bern, Switzerland. In J Mol Biol, 2006
The carboxy-terminal domain (CTD)of eIF5 is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure.
The joining of ribosomal subunits in eukaryotes requires eIF5B.
Hellen et al., New York City, United States. In Nature, 2000
eIF5 stimulates hydrolysis of eIF2-bound GTP and eIF2 is released from the 48S complex formed at the initiation codon before it is joined by a 60S subunit to form an active 80S ribosome.
share on facebooktweetadd +1mail to friends