The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells

Zhang J, Gurusaran M, Fujiwara Y, Zhang K, Echbarthi M, Vorontsov E, Guo R, Pendlebury D, Alam I, Livera G, Emmanuelle M, Wang P, Nandakumar J, Davies O, Shibuya H, Nature Communications 11(1) (2020) DOI

SASDH99 – Meiotic localizer of BRCA2 bound to BRME1 - MEILB2a1+2-BRME1 2:2 complex

BRME1
Meiotic localizer of BRCA2
MWexperimental 53 kDa
MWexpected 48 kDa
VPorod 104 nm3
log I(s) 9.49×10-2 9.49×10-3 9.49×10-4 9.49×10-5
BRME1 Meiotic localizer of BRCA2 small angle scattering data  s, nm-1
ln I(s)
BRME1 Meiotic localizer of BRCA2 Guinier plot ln 9.50×10-2 Rg: 5 nm 0 (5 nm)-2 s2
(sRg)2I(s)/I(0)
BRME1 Meiotic localizer of BRCA2 Kratky plot 1.104 0 3 sRg
p(r)
BRME1 Meiotic localizer of BRCA2 pair distance distribution function Rg: 5.3 nm 0 Dmax: 19 nm

Data validation


Fits and models


log I(s)
 s, nm-1
BRME1 Meiotic localizer of BRCA2 DAMMIF model
BRME1 Meiotic localizer of BRCA2 DAMMIF model

Synchrotron SAXS data from solutions of the meiotic localizer of BRCA2 bound to BRME1 (MEILB2a1+2-BRME1 2:2 complex) in 20 mM Tris pH 8.0, 150 mM KCl were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a wavelength of λ = 0.095 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 100 μl sample at 10 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 20 successive 3 second frames were collected through the sample elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank from the SEC-elution was subtracted.

BRME1 (BRME1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   11.4 kDa
 
UniProt   E9QNR8 (514-595)
Sequence   FASTA
 
Meiotic localizer of BRCA2 (MEILB2)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   12.8 kDa
 
UniProt   A0A3T0ZJB3 (18-122)
Sequence   FASTA