期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 13, 期 3, 页码 250-255出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1050
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资金
- Intramural NIH HHS Funding Source: Medline
- NCI NIH HHS [Z01 BC010309-07] Funding Source: Medline
- NCRR NIH HHS [P20 RR016476, RR016476] Funding Source: Medline
H1 linker histones stabilize the nucleosome, limit nucleosome mobility and facilitate the condensation of metazoan chromatin. Here, we have combined systematic mutagenesis, measurement of in vivo binding by photobleaching microscopy, and structural modeling to determine the binding geometry of the globular domain of the H1(0) linker histone variant within the nucleosome in unperturbed, native chromatin in vivo. We demonstrate the existence of two distinct DNA-binding sites within the globular domain that are formed by spatial clustering of multiple residues. The globular domain is positioned via interaction of one binding site with the major groove near the nucleosome dyad. The second site interacts with linker DNA adjacent to the nucleosome core. Multiple residues bind cooperatively to form a highly specific chromatosome structure that provides a mechanism by which individual domains of linker histones interact to facilitate chromatin condensation.
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