Histone H1-DNA Interaction: Structure, Function and Cellular Role

This report provides a comprehensive overview of the interaction between histone H1 protein and DNA, highlighting its critical role in chromatin structure and gene regulation. The report details how histone H1 interacts with DNA to compact it, influencing gene expression, and facilitating chromosomal segregation during the cell cycle. It describes the tripartite structure of histone H1, including its domains involved in DNA binding and stabilization of chromatin fibers. The report also discusses the impact of this interaction on DNA condensation, homologous recombination, and DNA repair, as well as the potential for artificial manipulation through epigenetic drugs. The importance of this interaction is emphasized, as it is essential for the efficient packaging of DNA within the nucleus and the regulation of gene expression. The report further explains how the absence of this interaction can lead to DNA distortion, improper segregation of genetic material, and compromised gene expression. Finally, the report references multiple sources to support its claims and to provide further information on the subject.

Running head: HISTONE H1-DNA INTERACTION
HISTONE H1-DNA INTERACTION
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1HISTONE H1-DNA INTERACTION
Linker histone H1 is the chromatin protein which interacts with the DNA and results in
its compaction and modification in structure. The interaction between them is known to stabilize
the chromatin structure. DNA is present as the loose thread in the nucleus of the cell at the
prophase stage of the cell. Its packaging is essential for its expression and protein synthesis
(Turner et al. 2018). The interaction of histone protein and DNA results in its compaction where
they bound with each other through covalent bonds. Such structure is called nucleosomes, where
H2A, H2B, H3 and H4 protein takes place (Li et al. 2018). Linker histone H1 proteins are not
part of nucleosome, they interact with linker DNA, and nucleosome dyad thus stabilizes the
30nm chromatin fiber. It makes the DNA more compact and promotes solenoid like chromatin
fiber. The primary function of such interaction is the regulation of expression of the gene. The
interaction of H1 histone protein and DNA is required for chromosomal segregation during the
cell cycle (Izzo et al. 2016). They are known to downregulate the transcription and replication of
DNA by promoting more compacted chromatin architecture. H1-DNA interaction makes DNA
more condensed and represses homologous recombination and repair of DNA damage
(Thorslund et al. 2015). There are many genes whose expression leads to cancer or other
diseases. Its expression is halted with such interactions. Such a condensed state of DNA makes
heterochromatin.
Histone H1 is having tripartite structure made up of three domain they are N-terminal
domain (NTD), central globular domain (GD) and C-terminal domain (CTD). The central folded
globular domain has DNA binding domain which interacts with nucleosomes and CTD connects
the linker DNA. DNA being negatively charge binds tightly with positively charge CTD and
NTD of H1 protein (Roque, Ponte and Suau 2016).

2HISTONE H1-DNA INTERACTION
Thus, it stabilizes the high order structure of chromatin. Such interaction does not have
clear structure, and they are regarded as intrinsically disordered and flexible (Torres et al. 2016).
It allows to accommodate according to the site of interaction with nucleic acid and gain
secondary structure (Chen et al. 2017).
The interaction takes place during cell cycle where the DNA is compacted to get
segregated. During the phases of the cell cycle, the DNA starts to get modify and condensed in
order to fit in the nucleus. The compacted DNA results in the proper division of genetic material.
Thus, from this, it is known that it takes place in the nucleus of cells (Shimamoto et al. 2017).
If such interaction does not happen, DNA being 2 meters would be able to get
accommodated in 100 μm diameter cell (Basu et al. 2019). The stabilization of DNA will have
been affected if such interaction is absent. Equal segregation of genetic material in the cell
during cell division would not take place and result in distortion of DNA inside in the nucleus.
Further, the regulation of gene expression would be compromised, causing a high level of
expression of unwanted genes. (Flanagan and Brown 2016).
The interaction of histone H1 and DNA can be artificially manipulated. For example, by
addition of Epi-drugs such as HDAC inhibitor can affect the modification of H1 making the
DNA accessible for expression (Brockers and Schneider 2019).

3HISTONE H1-DNA INTERACTION
Reference
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Ha, T., 2019. Measuring the Physical Properties of DNA on a Genomic Scale. Biophysical
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Brockers, K. and Schneider, R., 2019. Histone H1, the forgotten histone.
Chen, Q., Yang, R., Korolev, N., Liu, C.F. and Nordenskiöld, L., 2017. Regulation of
nucleosome stacking and chromatin compaction by the histone H4 N-terminal tail–H2A acidic
patch interaction. Journal of molecular biology, 429(13), pp.2075-2092.
Flanagan, T.W. and Brown, D.T., 2016. Molecular dynamics of histone H1. Biochimica et
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Izzo, A. and Schneider, R., 2016. The role of linker histone H1 modifications in the regulation of
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Li, Y., Li, Z., Dong, L., Tang, M., Zhang, P., Zhang, C., Cao, Z., Zhu, Q., Chen, Y., Wang, H.
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function. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1859(3), pp.444-
454.

4HISTONE H1-DNA INTERACTION
Shimamoto, Y., Tamura, S., Masumoto, H. and Maeshima, K., 2017. Nucleosome–nucleosome
interactions via histone tails and linker DNA regulate nuclear rigidity. Molecular biology of the
cell, 28(11), pp.1580-1589.
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