2020
DOI: 10.1101/2020.12.20.423657
|View full text |Cite
Preprint
|
Sign up to set email alerts
|

Linker histone H1.8 inhibits chromatin-binding of condensins and DNA topoisomerase II to tune chromosome length and individualization

Abstract: SummaryDNA loop extrusion by condensins and decatenation by DNA topoisomerase II (topo II) drive mitotic chromosome compaction and individualization. Here, we reveal that the linker histone H1.8 regulates chromatin levels of condensins and topo II. In vitro chromatin reconstitution experiments demonstrate that H1.8 inhibits binding of condensins and topo II to nucleosome arrays. Accordingly, H1.8 depletion in Xenopus egg extracts increased condensins and topo II levels on mitotic chromatin. Chromosome morpholo… Show more

Help me understand this report
View published versions

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
9
0

Year Published

2021
2021
2022
2022

Publication Types

Select...
3
2

Relationship

0
5

Authors

Journals

citations
Cited by 6 publications
(10 citation statements)
references
References 173 publications
(346 reference statements)
1
9
0
Order By: Relevance
“…For example, a recent study of mitotic chromosome condensation [ 167 ] explored the interaction between linker histone (regulator of short-range chromatin fiber behavior that binds individual nucleosomes) and condensins (large ring-like complexes with ATPase activity that can extrude loops of DNA) [ 168 ]. In vitro , linker histone inhibits condensin binding to nucleosome arrays, which has been proposed to play a role in tuning the compaction and topology of mitotic chromosomes [ 167 ]. Thus, it is important to consider both the distinctions and the connections in compaction at different length scales.…”
Section: Regulation Of Accessibility By the Chromatin Fiber And Nucle...mentioning
confidence: 99%
“…For example, a recent study of mitotic chromosome condensation [ 167 ] explored the interaction between linker histone (regulator of short-range chromatin fiber behavior that binds individual nucleosomes) and condensins (large ring-like complexes with ATPase activity that can extrude loops of DNA) [ 168 ]. In vitro , linker histone inhibits condensin binding to nucleosome arrays, which has been proposed to play a role in tuning the compaction and topology of mitotic chromosomes [ 167 ]. Thus, it is important to consider both the distinctions and the connections in compaction at different length scales.…”
Section: Regulation Of Accessibility By the Chromatin Fiber And Nucle...mentioning
confidence: 99%
“…At least, our theory provides insight into the mechanism of the assembly of the reconstituted chromosomes, which have been studied intensively in recent years. [12][13][14]29,32…”
Section: Discussionmentioning
confidence: 99%
“…For simplicity, we here treat cases in which the loading rate of condensin molecules is relatively small and they do not form nested loops, see also Discussion. Condensin is not loaded to the DNA binding sites that are already bound by linker histones, 29 but can be loaded to unoccupied DNA binding sites with equal probability. In this paper, we treat cases in which the concentration of linker histones is relatively small, ϵ − µ > 0, and the binding between DNA and linker histones is stabilized by the interaction energy (the third term of eq.…”
Section: Loop Extrusion Dynamicsmentioning
confidence: 99%