With nucleosomes alone, neither competitor substantially removes the main nucleosome band, although some free labelled DNA is present. With nucleosome–NVNA1 complexes, increasing specific competitor DNA removes the extra shifts and restores the nucleosome band. The starting shifted complexes therefore contained histones as well as NVNA1: competitor recognition sites draw NVNA1 away while leaving labelled DNA associated with histones.
nonspecific competitor DNA gives a different endpoint. The shifted population changes to a band matching the far-right NVNA1–naked-DNA control, rather than returning mainly to the nucleosome position. The labelled DNA remains bound to NVNA1 while histones can transfer to the excess competitor DNA. NVNA1 binding destabilizes the nucleosome against competitor-induced histone displacement. Remaining shifted DNA is not evidence that the histone octamer remained: its mobility must be compared with both controls. The nucleosome-only competition lanes show that competitor DNA alone is insufficient to cause the same conversion. Histone-specific detection would confirm the inferred component loss. A closely analogous ternary-complex and competition analysis was demonstrated for EBNA1; it provides a methodological precedent without establishing the identity of NV.[ref]
Epstein–Barr nuclear antigen 1 binds and destabilizes nucleosomes at the viral origin of latent DNA replication by Tina M. Avolio-Hunter and others. Figures 2–4: ternary complexes, specific competition and histone displacement
Tina M. Avolio-Hunter Created 2026-10-20 Updated 2026-11-05
DNA replication copies a double-stranded DNA molecule into two daughter double-stranded DNA molecules. In semiconservative replication, each daughter retains one parental strand and receives one newly synthesized complementary strand. DNA polymerases build the new strands from incoming nucleotides; they do not make RNA or proteins in this copying step. See Alberts et al., Molecular Biology of the Cell, 4th edition (2002): DNA replication mechanisms.