Tobias Raisch
@traisch.bsky.social
Biochemist and Structural Biologist | Project group leader MPI Dortmund | He/him | Vegan bike punk #LeaveNoOneBehind
A tiny difference in the nucleosome structures is that once the second MPO unit is present, there would be a clash with the DNA terminus.
As a consequence, in the presence of MPO dimer the DNA has to locally unwrap and becomes disordered, as visible in this morph:
As a consequence, in the presence of MPO dimer the DNA has to locally unwrap and becomes disordered, as visible in this morph:
September 18, 2025 at 3:39 PM
A tiny difference in the nucleosome structures is that once the second MPO unit is present, there would be a clash with the DNA terminus.
As a consequence, in the presence of MPO dimer the DNA has to locally unwrap and becomes disordered, as visible in this morph:
As a consequence, in the presence of MPO dimer the DNA has to locally unwrap and becomes disordered, as visible in this morph:
We then reconstituted nucleosomes with a recombinant MPO that resembles a monomeric precursor of native (dimeric) MPO.
By #CryoEM, we saw that MPO stably binds to the acidic patch of the nucleosome, an a binding mode similar to many other nucleosome interactors.
By #CryoEM, we saw that MPO stably binds to the acidic patch of the nucleosome, an a binding mode similar to many other nucleosome interactors.
September 18, 2025 at 3:39 PM
We then reconstituted nucleosomes with a recombinant MPO that resembles a monomeric precursor of native (dimeric) MPO.
By #CryoEM, we saw that MPO stably binds to the acidic patch of the nucleosome, an a binding mode similar to many other nucleosome interactors.
By #CryoEM, we saw that MPO stably binds to the acidic patch of the nucleosome, an a binding mode similar to many other nucleosome interactors.