Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 126, Issue 36, Pages 6771-6779Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.2c03785
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Funding
- National Natural Science Foundation of China [92053202, 22050003]
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Research has found that protein gH1 has a sequence-dependent binding with DNA, leading to conformational changes in nucleosomes and affecting their compaction and accessibility of core histones. This finding is important for understanding gene regulation signals.
Sequence-dependent binding between DNA and proteins in chromatin is an essential part of gene expression. Linker histone H1 is an important protein in the regulation of chromatin compartmentalization and compaction, and its binding with the nucleosome is sensitive to the DNA sequence. Although the interactions of H1 and DNA have been widely investigated, the mechanism of nucleosome conformation changes induced by the DNA-sequence-dependent binding with gH1 (globular H1.0) remains largely unclear at the atomic level. In the present molecular dynamics simulations, both linker and dyad DNAs were mutated to investigate the conformational changes of the nucleosome induced by the sequence-dependent binding of gH1 based on the on-dyad binding mode. Our results indicate that gH1 is insensitive to the DNA sequence of the dyad DNA but presents an apparent preference to linker DNA with an AT-rich sequence. Moreover, this specific binding induces the entry/exit region of a nucleosome to a tight conformation and regulates the accessibility of core histones. Considering that the entry/exit region of the nucleosome is a crucial binding site for many functional proteins related to gene expression, the conformational change at this region could represent an important gene regulation signal.
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