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• W1969468131 abstract "Higher-order architectures of chromosomes play important roles in the regulation of genome functions. To understand the molecular mechanism of genome packing, an in vitro chromatin reconstitution method and a single-molecule imaging technique (atomic force microscopy) were combined. In 50 mM NaCl, well-stretched beads-on-a-string chromatin fiber was observed. However, in 100 mM NaCl, salt-induced interaction between nucleosomes caused partial aggregation. Addition of histone H1 promoted a further folding of the fiber into thicker fibers 20−30 nm in width. Micrococcal nuclease digestion of these thicker fibers produced an ∼170 bp fragment of nucleosomal DNA, which was ∼20 bp longer than in the absence of histone H1 (∼150 bp), indicating that H1 is correctly placed at the linker region. The width of the fiber depended on the ionic strength. Widths of 20 nm in 50 mM NaCl became 30 nm as the ionic strength was changed to 100 mM. On the basis of these results, a flexible model of chromatin fiber formation was proposed, where the mode of the fiber compaction changes depending both on salt environment and linker histone H1. The biological significance of this property of the chromatin architecture will be apparent in the closed segments (∼100 kb) between SAR/MAR regions." @default.
• W1969468131 created "2016-06-24" @default.
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• W1969468131 date "2005-09-03" @default.
• W1969468131 modified "2023-10-17" @default.
• W1969468131 title "Linker Histone H1 per se Can Induce Three-Dimensional Folding of Chromatin Fiber" @default.
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• W1969468131 doi "https://doi.org/10.1021/bi050623v" @default.
• W1969468131 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16185066" @default.
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