eIF3j is located in the decoding center of the human 40S ribosomal subunit.

By C. Fraser, Katherine E. Berry, J. Hershey, Jennifer A. Doudna. 2007

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Citations in the corpus

Protein Synthesis Initiation in Eukaryotic Cells. (2018, background): “3) (Fraser et al. 2007; Aylett et al. 2015). eIF3j binding was shown to impair mRNA recruitment to 40S, except when TC was present, suggesting eIF3j may impair mRNA binding to 40S complexes lacking TC (Fraser et al. 2007; Mitchell et al. 2010).”
A structural inventory of native ribosomal ABCE1‐43S pre‐initiation complexes (2020, unknown): “This position explains, how eIF3j could exert its roles as an antagonist of mRNA binding, for example by recycling of mRNA from the 40S subunit (Pisarev et al , 2007; Pisarev et al , 2010), or during initiation by preventing premature mRNA recruitment (Fraser et al , 2007).”
THE MECHANISM OF EUKARYOTIC TRANSLATION INITIATION AND PRINCIPLES OF ITS REGULATION (2010, background): “mRNA activation, during which the mRNA cap-proximal region is unwound in an ATP-dependent manner by eIF4F with eIF4B (4); attachment of the 43S complex to this mRNA region (5); scanning of the 5′ UTR in a 5′ to 3′ direction by 43S complexes (6);”
Toward a Kinetic Understanding of Eukaryotic Translation. (2018, background): “This is likely due to the fact that eIF3j binds to the mRNA entry channel and A site of the 43S PIC with a reduced affinity when mRNA is stabilized in the mRNA entry channel (Unbehaun et al. 2004; Fraser et al. 2007; Aylett et al. 2015; Sharifulin et al. 2016).”
The scanning mechanism of eukaryotic translation initiation. (2014, background): “However, because much of eIF3 is flexible, it may communicate dynamically with factors bound to the interface side of the 40S subunit (83), which would accord with A-site binding of meIF3j-CTD (93) and interactions between yeIF3 subunits and eIF1, -2, and -5 in the multifactor complex (MFC) that pro”
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets (2009, unknown): “Interestingly, the j-subunit of eIF3 can bind near the A-site and mRNA entry channel of the 40S subunit and impede mRNA binding in the absence of TC, presumably to ensure that TC loading precedes 40S binding to mRNA (Fraser et al., 2007).”
Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation. (2017, background): “The CTD of mammalian 3j can bind directly to the 40S mRNA entry channel in a manner anticooperative with eIF1A binding in the A site [86].”
The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit (2011, methodology): “Human initiator tRNA was in vitro transcribed by T7 RNA polymerase and charged with either non-labeled or (35)S-labeled methionine using Escherichia coli methionyl-tRNA synthetase as described previously (15).”
RACK1 on and off the ribosome (2019, methodology): “(Fraser et al. 2007) The ORF from human RACK1 was subcloned from the lentivirus expression construct, the ORF for P. falciparum RACK1 (PfRACK1) was subcloned from P. falciparum asexual stage cDNA from the D10 strain (a gift from Michael Boucher, Ellen Yeh lab), and the ORF for S. cerevisiae Asc1p…”
Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B (2011, methodology): “Human eIF4B (611 amino acids) is inserted into a modified His-tagged pFASTBAC1 vector (Invitrogen) and expressed in insect cells (sf9), as described previously for human eIF3j.(44) Expression and initial purification of each protein using Ni-NTA Superflow resin (Qiagen) are carried out using a stand”
Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity (2013, methodology): “Briefly, recombinant eIF4A isoform I (eIF4AI), 4EBP1, eIF4G682–1105, and PABP proteins are expressed in bacteria as maltosebinding protein fusion constructs, cleaved by using recombinant tobacco etch virus (TEV) protease, and purified by using established procedures to generate untagged proteins (21”