Rev7 dimerization is important for assembly and function of the Rev1/PolĪ¶ translesion synthesis complex.

Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM, Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018) Europe PMC

SASDC69 – Human Rev7 dimer in complex with Rev3 peptide @ 4.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2B
DNA polymerase zeta catalytic subunit
DNA polymerase zeta catalytic subunit
MWI(0) 50 kDa
MWexpected 55 kDa
log I(s) 1.45×10-1 1.45×10-2 1.45×10-3 1.45×10-4
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit small angle scattering data  s, nm-1
ln I(s)
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Guinier plot ln 1.45×10-1 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot 1.104 0 3 sRg

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Human Rev7 dimer in complex with Rev3 peptide @ 4.6mg/mL in 20 mM HEPES, 10 mM DTT, 5% glycerol, pH 8 were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS) storage ring (Ithaca, NY, USA) using a Finger Lakes CCD detector at a wavelength of λ = 0.1267 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.60 mg/ml was measured at 4°C. 10 successive 1 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.

Based on the affinity of the Rev7 dimer, at this concentration (and below) there is a mixture of monomer and dimer in the solution. This dataset was not used for modeling

Mitotic spindle assembly checkpoint protein MAD2B (hRev7-WT dimer)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   24.4 kDa
 
UniProt   Q9UI95 (1-211)
Sequence   FASTA
 
DNA polymerase zeta catalytic subunit (Rev3-RBM2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   3.3 kDa
 
UniProt   O60673 (1988-2014)
Sequence   FASTA
 
DNA polymerase zeta catalytic subunit (Rev3-RBM2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   3.3 kDa
 
UniProt   O60673 (1988-2014)
Sequence   FASTA