eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation.

Schmidt T, Dabrowska A, Waldron JA, Hodge K, Koulouras G, Gabrielsen M, Munro J, Tack DC, Harris G, McGhee E, Scott D, Carlin LM, Huang D, Le Quesne J, Zanivan S, Wilczynska A, Bushell M, Nucleic Acids Res (2023) Europe PMC

SASDQU6 – eukaryotic initiation factor 4A1 bound to 20 nt (AG)10 ssRNA

Eukaryotic initiation factor 4A-I
(AG)10-RNA
MWexperimental 55 kDa
MWexpected 53 kDa
VPorod 96 nm3
log I(s) 5.26×10-2 5.26×10-3 5.26×10-4 5.26×10-5
Eukaryotic initiation factor 4A-I (AG)10-RNA small angle scattering data  s, nm-1
ln I(s)
Eukaryotic initiation factor 4A-I (AG)10-RNA Guinier plot ln 5.27×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Eukaryotic initiation factor 4A-I (AG)10-RNA Kratky plot 1.104 0 √3 sRg
p(r)
Eukaryotic initiation factor 4A-I (AG)10-RNA pair distance distribution function Rg: 2.8 nm 0 Dmax: 10.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of eukaryotic initiation factor 4A1 bound to 20 nt (AG)10 ssRNA in 20 mM Hepes, 100 mM KCl, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 4°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Eukaryotic initiation factor 4A-I
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   46.2 kDa
 
UniProt   P60842 (1-406)
Sequence   FASTA
 
(AG)10-RNA (AG10)
Mol. type   RNA
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   6.8 kDa
Sequence   FASTA