Single-stranded nucleic acid binding and coacervation by linker histone H1-Reference-Cited by-同舟云学术

Single-stranded nucleic acid binding and coacervation by linker histone H1

Published:2022-04-28 Issue:5 Volume:29 Page:463-471
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Leicher Rachel^ORCID,Osunsade Adewola^ORCID,Chua Gabriella N. L.,Faulkner Sarah C.,Latham Andrew P.^ORCID,Watters John W.^ORCID,Nguyen Tuan,Beckwitt Emily C.,Christodoulou-Rubalcava Sophia,Young Paul G.,Zhang Bin^ORCID,David Yael^ORCID,Liu Shixin^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

https://www.nature.com/articles/s41594-022-00760-4.pdf

Reference68 articles.

1. Woodcock, C. L., Skoultchi, A. I. & Fan, Y. Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res 14, 17–25 (2006).

2. Song, F. et al. Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units. Science 344, 376–380 (2014).

3. Bednar, J. et al. Structure and dynamics of a 197 bp nucleosome in complex with linker histone H1. Mol. Cell 66, 384–397 e8 (2017).

4. Zhou, B. R. et al. Distinct structures and dynamics of chromatosomes with different human linker histone isoforms. Mol. Cell 81, 166–182 e6 (2021).

5. Rudnizky, S. et al. Extended and dynamic linker histone-DNA Interactions control chromatosome compaction. Mol. Cell 81, 3410–3421 e4 (2021).

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