Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation.

The EMBO journal - 1 May 2001

Asano K, Shalev A, Phan L, Nielsen K, Clayton J, Valásek L, Donahue T F, Hinnebusch A G

Abstract excerpt

eIF5 stimulates the GTPase activity of eIF2 bound to Met-tRNA(i)(Met), and its C-terminal domain (eIF5-CTD) bridges interaction between eIF2 and eIF3/eIF1 in a multifactor complex containing Met-tRNA(i)(Met). The tif5-7A mutation in eIF5-CTD, which destabilizes the multifactor complex in vivo, reduced the binding of Met-tRNA(i)(Met) and mRNA to 40S subunits in vitro. Interestingly, eIF5-CTD bound simultaneously...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Codon, Initiator
Share to Eukaryotic Initiation Factor-2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Eukaryotic Initiation Factor-3

Share to Eukaryotic Initiation Factor-4G

Share to Guanosine Triphosphate

Share to Peptide Initiation Factors

Share to Poly A

Share to RNA, Transfer, Met

Source

Open in PubMed Open full text

Identifiers

PMID: 11331597
DOI: 10.1093/emboj/20.9.2326
PMCID: PMC125443

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation.PMID 11331597Read ↗

Physical association of eukaryotic initiation factor (eIF) 5 carboxyl-terminal domain with the lysine-rich eIF2beta segment strongly enhances its binding to eIF3.Semantic proximity Read ↗

Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection.Semantic proximity Read ↗

Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo.Semantic proximity Read ↗

An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation.Semantic proximity Read ↗

Sequential 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.Semantic proximity Read ↗

Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.Semantic proximity Read ↗

The eIF1A C-terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo.Semantic proximity Read ↗

The C-terminal domain of eukaryotic initiation factor 5 promotes start codon recognition by its dynamic interplay with eIF1 and eIF2β.Semantic proximity Read ↗

Eukaryotic translation initiation factor eIF5 promotes the accuracy of start codon recognition by regulating Pi release and conformational transitions of the preinitiation complex.Semantic proximity Read ↗

Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation.Semantic proximity Read ↗

eIF5 and eIF5B together stimulate 48S initiation complex formation during ribosomal scanning.Semantic proximity Read ↗

Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.