Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein.

Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J, Nucleic Acids Res (2023) Europe PMC

SASDNN8 – Upstream of N-ras, isoform A, CSD 7, 8 and 9 from Drosophila melanogaster in complex with a poly(A)-15mer RNA

Upstream of N-ras, isoform A
polyA-15mer
MWI(0) 29 kDa
MWexpected 31 kDa
VPorod 37 nm3
log I(s) 2.88×10-2 2.88×10-3 2.88×10-4 2.88×10-5
Upstream of N-ras, isoform A polyA-15mer small angle scattering data  s, nm-1
ln I(s)
Upstream of N-ras, isoform A polyA-15mer Guinier plot ln 2.88×10-2 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Upstream of N-ras, isoform A polyA-15mer Kratky plot 1.104 0 √3 sRg
p(r)
Upstream of N-ras, isoform A polyA-15mer pair distance distribution function Rg: 2.3 nm 0 Dmax: 7.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of N-ras, isoform A in complex with a poly(A)-15mer RNA in 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.5 and 5.8 mg/ml were measured at 20°C. 20 successive 0.195 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Upstream of N-ras, isoform A (Unr)
Mol. type   Protein
Organism   Drosophila melanogaster
Olig. state   Monomer
Mon. MW   26.2 kDa
 
UniProt   Q9VSK3 (757-991)
Sequence   FASTA
 
polyA-15mer
Mol. type   RNA
Olig. state   Monomer
Mon. MW   5.0 kDa
Sequence   FASTA