Abstract
Linker histone H1.2, which belongs to the linker histone family H1, plays a crucial role in the maintenance of the stable higher-order structures of chromatin and nucleosomes. As a critical part of chromatin structure, H1.2 has an important function in regulating chromatin dynamics and participates in multiple other cellular processes as well. Recent work has also shown that linker histone H1.2 regulates the transcription levels of certain target genes and affects different processes as well, such as cancer cell growth and migration, DNA duplication and DNA repair. The present work briefly summarizes the current knowledge of linker histone H1.2 modifications. Further, we also discuss the roles of linker histone H1.2 in the maintenance of genome stability, apoptosis, cell cycle regulation, and its association with disease.
Highlights
The genomic DNA in eukaryotes lies packaged inside the nucleus in a highly complicated structure involving chromatin fiber, nucleoproteins, and repeating nucleosome arrays
It has been shown that ITCH mediated H1.2 K46 ubiquitination suppresses DNA damage repair by impairing RNF8/RNF168-dependent formation of 53BP1 foci, which is a crucial component of nonhomologous end-joining (NHEJ) signaling (Chang et al, 2019)
This study indicates that H1.2 is evicted from sites of DNA damage and H1.2 maintains chromatin stability while allowing for a less compact chromatin configuration so DNA repair enzymes can access the site of damage (Figure 3)
Summary
The genomic DNA (gDNA) in eukaryotes lies packaged inside the nucleus in a highly complicated structure involving chromatin fiber, nucleoproteins, and repeating nucleosome arrays. The function of the C-terminal and the globular domain is to bind H1 to the nucleosome and to maintain the compact higher-order (30-nm) chromatin structure (Fyodorov et al, 2018; Hendzel et al, 2004; Robinson and Rhodes, 2006). Since the N-terminal domain is rich in alanine and proline, as well as other hydrophobic amino acids, it does not have a high affinity for DNA Both the N-terminal tail and the globular domain in linker histone H1 may undergo diverse post-translational modifications (PTMs), which have key functions in modulating the function and structure of chromatin (Fyodorov et al, 2018). Its relations with some common disorders are analyzed to shed more light on possible new therapeutic targets
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