Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1.

Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA, Nucleic Acids Res (2021) Europe PMC

SASDJM5 – Modified nucleolysin TIA-1 isoform p40 (TIA-1 APO)

Modified Nucleolysin TIA-1 isofrom p40
MWexperimental 38 kDa
MWexpected 42 kDa
VPorod 62 nm3
log I(s) 5.10×10-2 5.10×10-3 5.10×10-4 5.10×10-5
Modified Nucleolysin TIA-1 isofrom p40 small angle scattering data  s, nm-1
ln I(s)
Modified Nucleolysin TIA-1 isofrom p40 Guinier plot ln 5.10×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Modified Nucleolysin TIA-1 isofrom p40 Kratky plot 1.104 0 3 sRg
p(r)
Modified Nucleolysin TIA-1 isofrom p40 pair distance distribution function Rg: 3.4 nm 0 Dmax: 12.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of modified TIA-1 in 20 mM sodium phosphate, 60 mM KCl, 0.5 M arginine-HCl, 1 mM MgCl2, 2 mM DTT, 0.5 mM EDTA, pH 7 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 1.4 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 30 successive 1 second frames were collected from samples at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Modified Nucleolysin TIA-1 isofrom p40
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   42.2 kDa
Sequence   FASTA