Mutations in GCD11, the structural gene for eIF-2 gamma in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis.
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Recognition of 5'-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2.A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivoAn aminoacylation-dependent nuclear tRNA export pathway in yeastSequential eukaryotic translation initiation factor 5 (eIF5) binding to the charged disordered segments of eIF4G and eIF2β stabilizes the 48S preinitiation complex and promotes its shift to the initiation mode.eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selectionLigand interactions with eukaryotic translation initiation factor 2: role of the gamma-subunitThe beta subunit of eukaryotic translation initiation factor 2 binds mRNA through the lysine repeats and a region comprising the C2-C2 motif.Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNATranslation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits.Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5Cryo-EM study of start codon selection during archaeal translation initiationRecognition of AUG and alternative initiator codons is augmented by G in position +4 but is not generally affected by the nucleotides in positions +5 and +6.Minimum requirements for the function of eukaryotic translation initiation factor 2.Components of the multifactor complex needed for internal initiation by the IRES of hepatitis C virus in Saccharomyces cerevisiaeStructure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 regionMolecular mechanism of scanning and start codon selection in eukaryotes.Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAi(Met) ternary complex binding to the 40S ribosome.The β-hairpin of 40S exit channel protein Rps5/uS7 promotes efficient and accurate translation initiation in vivo.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.Translation initiation factor 2gamma mutant alters start codon selection independent of Met-tRNA binding.Two genes become one: the genes encoding heterochromatin protein Su(var)3-9 and translation initiation factor subunit eIF-2gamma are joined to a dicistronic unit in holometabolic insects.Conserved sequences in the beta subunit of archaeal and eukaryal translation initiation factor 2 (eIF2), absent from eIF5, mediate interaction with eIF2gamma.Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange.
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P2860
Mutations in GCD11, the structural gene for eIF-2 gamma in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1995
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Mutations in GCD11, the struct ...... rt site for protein synthesis.
@en
Mutations in GCD11, the struct ...... rt site for protein synthesis.
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type
label
Mutations in GCD11, the struct ...... rt site for protein synthesis.
@en
Mutations in GCD11, the struct ...... rt site for protein synthesis.
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prefLabel
Mutations in GCD11, the struct ...... rt site for protein synthesis.
@en
Mutations in GCD11, the struct ...... rt site for protein synthesis.
@nl
P2860
P1433
P1476
Mutations in GCD11, the struct ...... art site for protein synthesis
@en
P2093
Erickson FL
P2860
P304
P356
10.1002/J.1460-2075.1995.TB07218.X
P407
P577
1995-05-01T00:00:00Z