Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex.

Sabine R Akabayov, Barak Akabayov, Gerhard Wagner

Open access · greenAbstract readComparative Study

In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it

0cells of the map it votes in

2citing papers in PubMed

–field-weighted citation impact, top 94% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 2 citations in OpenAlex.

Auxiliary ATP binding sites support DNA unwinding by RecBCD.Nature communications · 2022
Article
EIF4G1 is a novel candidate gene associated with severe asthenozoospermia.Molecular genetics & genomic medicine · 2019
Article

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Sabine R AkabayovDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School , Longwood Avenue, Boston, Massachusetts 02115, United States.

Barak Akabayov

Gerhard Wagner

Harvard University · USBen-Gurion University of the Negev · IL

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017

$28.6M

STRUCTURAL BASIS OF TRANSLATION INITIATION BY EIF-4ER01CA068262 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2015

$3.6M

NCI NIH HHS R01 CA068262NCI NIH HHS R01CA068262NIGMS NIH HHS P01 GM047467NIGMS NIH HHS P01GM047467

6 · The paper itself

Abstract

Eukaryotic translation initiation factor 4G (eIF4G) plays a crucial role in translation initiation, serving as a scaffolding protein binding several other initiation factors, other proteins, and RNA. Binding of eIF4G to the ATP-dependent RNA helicase eukaryotic translation initiation factor 4A (eIF4A) enhances the activity of eIF4A in solution and in crowded environments. Previously, this activity enhancement was solely attributed to eIF4G, conferring a closed, active conformation upon eIF4A. Here we show that eIF4G contains a low-affinity binding site at the entrance to the ATP-binding cleft on eIF4A, suggesting that regulation of the local ATP concentration may be an additional reason for the enhancement in activity.

Indexed as

Models, MolecularAdenosine TriphosphateBinding SitesEnzyme InhibitorsEukaryotic Initiation Factor-4AEukaryotic Initiation Factor-4GFungal ProteinsHumansIntracellular SpaceKineticsMagnesiumManganeseNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Structure, SecondaryRecombinant ProteinsAdenosine TriphosphateEIF4G1 protein, humanEnzyme InhibitorsEukaryotic Initiation Factor-4AEukaryotic Initiation Factor-4GFungal ProteinsMagnesiumManganeseRecombinant ProteinsSaccharomyces cerevisiae ProteinsTIF4631 protein, S cerevisiae

Identifiers

PMID25255371

DOI10.1021/bi500600m

PMCPMC4204880

OpenAlexW1983726200

What OpenQuestion holds

Textmetadata

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.