Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.

Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M, Nat Commun 11(1):2905 (2020) Europe PMC

SASDGC3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 5.5)

80bp_DNA Forward
80bp_DNA Reverse
DNA-binding protein HU-alpha, E34K
MWexperimental 69 kDa
MWexpected 69 kDa
log I(s)
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K small angle scattering data  s, nm-1
(sRg)2I(s)
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K Kratky plot 0 3 sRg

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of DNA-binding protein HU-alpha (E34K mutant) bound to 80 bp DNA in 10 mM Bis-Tris, 50 mM NaCl, pH 5.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 300 successive 3 second frames were collected at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

His curve is part of a pH series. Increasing the pH removes aggregation presumably due to protein surface charge changes. The SAXS data for this entry is measured from aggregated material and therefore the Rg and I(0) parameters do not apply.

80bp_DNA Forward
Mol. type   DNA
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   24.8 kDa
Sequence   FASTA
 
80bp_DNA Reverse
Mol. type   DNA
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   24.6 kDa
Sequence   FASTA
 
DNA-binding protein HU-alpha, E34K
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   9.5 kDa
 
UniProt   P0ACF0 (1-90)
Sequence   FASTA