Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions.

Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS, Sci Adv 10(28):eadk6580 (2024) Europe PMC

SASDTP8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 150 MPa

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )
MWexperimental 30 kDa
MWexpected 25 kDa
log I(s) 1.23×10-1 1.23×10-2 1.23×10-3 1.23×10-4
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) small angle scattering data  s, nm-1
ln I(s)
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Guinier plot ln 1.23×10-1 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 150 MPa in 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH 7.5 were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS) storage ring (Ithaca, NY, USA) using a Eiger 4M detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.088 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 10 and 10 mg/ml were measured at 17°C. 10 successive 1 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.

CAUTION! Severely aggregated. CAUTION! Buffer scattering contributions likely over-subtracted.

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) (UP1 dm)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   24.9 kDa
 
UniProt   P09651 (1-196)
Sequence   FASTA