Abstract
The linker histone H1 family is the most abundant group of eukaryotic chromatin-binding proteins, in which H1 is known for its role as a nucleosome compactor and an essential component of higher order chromatin structure. However, the mechanism underlying the diverse physiological functions of H1 remains unclear. Here we used single-molecule fluorescence and force microscopy to observe the behavior of H1 on DNA under different tensions in real time. Unexpectedly, we observed that H1 preferentially coalesces around nascent single-stranded DNA, forming condensate-like complexes.
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