The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.

Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S, iScience 27(12):111259 (2024) Europe PMC

SASDSZ5 – DNA binding domain of PALB2 (partner and localizer of BRCA2) in 500 mM NaCl

Partner and localizer of BRCA2
MWexperimental 68 kDa
MWexpected 46 kDa
VPorod 171 nm3
log I(s) 2.33×10-2 2.33×10-3 2.33×10-4 2.33×10-5
Partner and localizer of BRCA2 small angle scattering data  s, nm-1
ln I(s)
Partner and localizer of BRCA2 Guinier plot ln 2.34×10-2 Rg: 5.5 nm 0 (5.5 nm)-2 s2
(sRg)2I(s)/I(0)
Partner and localizer of BRCA2 Kratky plot 1.104 0 3 sRg
p(r)
Partner and localizer of BRCA2 pair distance distribution function Rg: 5.8 nm 0 Dmax: 25.4 nm

Data validation


Fits and models


log I(s)
 s, nm-1
DNA binding domain of PALB2 (partner and localizer of BRCA2) in 500 mM NaCl Rg histogram Rg, nm

Synchrotron SAXS data from solutions of the DNA binding domain of PALB2 in 50 mM HEPES, 500 mM NaCl, 0.5 mM TCEP, pH 7.4 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Eiger2 XE 9M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.10332 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 300.00 μl sample at 8.2 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 23°C. 2500 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.

Partner and localizer of BRCA2 (PALB2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   22.9 kDa
 
UniProt   Q86YC2 (1-200)
Sequence   FASTA