WebJul 26, 2024 · CySC lineage eIF5 mediates cyst cell and germ cell differentiation. First of all, we analyzed the testicular eIF5 expression pattern via single nucleus RNA sequencing (snRNA-seq) data [] and found that eIF5 was widely expressed in Drosophila testes, especially in germ cells and cyst cells (Additional file 1: Fig. S1).To investigate the … WebFunction. function. Translation initiation regulator which represses non-AUG initiated translation and repeat-associated non-AUG (RAN) initiated translation by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function (By similarity). ... Increases the accuracy of translation initiation by impeding EIF5 ...
Translational control by 5′-untranslated regions of ... - Science
WebMay 20, 2010 · The invariant Arg 15 residue in eIF5 is critical for eIF5-dependent GAP activity and the eIF5 R15M mutation eliminates this function 6,7,8.The R15M mutant retains full eIF5 GDI activity (Fig. 1c ... • Das S, Maiti T, Das K, Maitra U (1998). "Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the beta-subunit of eIF2". J. Biol. Chem. 272 (50): 31712–8. doi:10.1074/jbc.272.50.31712. PMID 9395514. • Bandyopadhyay A, Maitra U (1999). "Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in mammalian cells". Nucleic Acids Res. 27 (5): 133… tractor supply company little river sc
eIF2 - Wikipedia
WebGTP-binding, Nucleotide-binding. Gene summary (Entrez)i. Useful information about the gene from Entrez. 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. WebThe translation factor eIF5 is an important partner of eIF2, directly modulating its function in several critical steps. First, eIF5 binds eIF2/GTP/Met-tRNA (i) (Met) ternary complex … WebMay 20, 2010 · Here we define new regulatory functions of eIF5 in the recycling of eIF2 from its inactive eIF2.GDP state between successive rounds of translation initiation. First we show that eIF5 stabilizes the binding of GDP to eIF2 and is therefore a bi-functional protein that acts as a GDP dissociation inhibitor (GDI). tractor supply company litchfield ct