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. Author manuscript; available in PMC: 2020 Nov 1.
Published in final edited form as: DNA Repair (Amst). 2019 Sep 16;83:102701. doi: 10.1016/j.dnarep.2019.102701

Figure 4: Dynamics of interactions of the acidic C-terminal tail of HMGB1 with Box A and Box B, and linker histone H1.

Figure 4:

The C-terminal tail of HMGB1 binds to the DNA-binding domains of HMGB1, restricting their interaction with DNA. However, the acidic tail of HMGB1 can interact with the basic tail of histone H1, thereby disrupting its interaction with the DNA-binding domains of HMGB1. This interaction can therefore lower the affinity of H1 for DNA and it can be displaced from the DNA by HMGB1, thereby facilitating binding of HMGB1 to DNA.