Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units

Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C, Proceedings of the National Academy of Sciences 120(42) (2023) DOI

SASDRK7 – M1-linked tetraubiquitin, M1(1-72)-Ub4

Polyubiquitin-B
MWI(0) 31 kDa
MWexpected 33 kDa
VPorod 41 nm3
log I(s) 2.16×10-2 2.16×10-3 2.16×10-4 2.16×10-5
Polyubiquitin-B small angle scattering data  s, nm-1
ln I(s)
Polyubiquitin-B Guinier plot ln 2.17×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Polyubiquitin-B Kratky plot 1.104 0 √3 sRg
p(r)
Polyubiquitin-B pair distance distribution function Rg: 3.4 nm 0 Dmax: 12.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of M1-linked tetraubiquitin, M1(1-72)-Ub4 in 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH 6.8 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.26 mg/ml was measured at 20°C. Six 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.

Polyubiquitin-B (M1(1-72)-Ub4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   33.1 kDa
 
UniProt   P0CG47 (1-72)
Sequence   FASTA