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

Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast.

Molecular and cellular biology - 1 Feb 2006

Jivotovskaya Antonina V, Valásek Leos, Hinnebusch Alan G, Nielsen Klaus H

Abstract excerpt

Recruitment of the eukaryotic translation initiation factor 2 (eIF2)-GTP-Met-tRNAiMet ternary complex to the 40S ribosome is stimulated by multiple initiation factors in vitro, including eIF3, eIF1, eIF5, and eIF1A. Recruitment of mRNA is thought to require the functions of eIF4F and eIF3, with the latter serving as an adaptor between the ribosome and the 4G subunit of eIF4F. To define the factor requirements for...

Read the complete abstract on PubMed

Topics

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

Share to Eukaryotic Initiation Factor-2
Share to Eukaryotic Initiation Factor-3

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Eukaryotic Initiation Factor-4G

Share to Eukaryotic Initiation Factors

Share to Genes, Fungal

Share to Protein Subunits

Share to Ribosomes

Share to RNA, Fungal

Source

Open in PubMed Open full text

Identifiers

PMID: 16449648
DOI: 10.1128/MCB.26.4.1355-1372.2006
PMCID: PMC1367198

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast.PMID 16449648Read ↗

Human eukaryotic initiation factor 4G directly binds the 40S ribosomal subunit to promote efficient translationSemantic proximity Read ↗

Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control.Semantic proximity Read ↗

Coupled release of eukaryotic translation initiation factors 5B and 1A from 80S ribosomes following subunit joining.Semantic proximity Read ↗

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

The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning.Semantic proximity Read ↗

A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)Met.Semantic proximity Read ↗

β-Hairpin loop of eukaryotic initiation factor 1 (eIF1) mediates 40 S ribosome binding to regulate initiator tRNA(Met) recruitment and accuracy of AUG selection in vivo.Semantic proximity Read ↗

Yeast eukaryotic initiation factor 4B (eIF4B) enhances complex assembly between eIF4A and eIF4G in vivo.Semantic proximity Read ↗

Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo.Semantic proximity Read ↗

Functional analysis of individual binding activities of the scaffold protein eIF4G.Semantic proximity Read ↗

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

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