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

SASDTC8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut); SEC-SAXS, July 2022)

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )
MWexperimental 43 kDa
MWexpected 34 kDa
VPorod 57 nm3
log I(s) 2.89×10-3 2.89×10-4 2.89×10-5 2.89×10-6
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) small angle scattering data  s, nm-1
ln I(s)
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Guinier plot ln 2.89×10-3 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot 1.104 0 3 sRg
Dmax: 14 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut); SEC-SAXS, July 2022) in 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH 7.5 were collected on the 12-ID-B beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Eiger2 S detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 200.00 μl sample at 12 mg/ml was injected at a 0.60 ml/min flow rate onto a Cytiva Superdex 200 Increase 10/300 column at 22°C. 2530 successive 0.500 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! Possible aggregation. CAUTION! Possible buffer scattering mismatch.

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) (hnRNP A1-A(mut))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   34.2 kDa
 
UniProt   P09651-2 (2-320)
Sequence   FASTA