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. 2014 Mar;7(3):481-91.
doi: 10.1093/mp/sst164. Epub 2013 Nov 22.

Open and closed: the roles of linker histones in plants and animals

Ryan S Over  1 , Scott D Michaels
Affiliations

Open and closed: the roles of linker histones in plants and animals

Ryan S Over et al. Mol Plant. 2014 Mar.

Abstract

Histones package DNA in all eukaryotes and play key roles in regulating gene expression. Approximately 150 base pairs of DNA wraps around an octamer of core histones to form the nucleosome, the basic unit of chromatin. Linker histones compact chromatin further by binding to and neutralizing the charge of the DNA between nucleosomes. It is well established that chromatin packing is regulated by a complex pattern of posttranslational modifications (PTMs) to core histones, but linker histone function is less well understood. In this review, we describe the current understanding of the many roles that linker histones play in cellular processes, including gene regulation, cell division, and development, while putting the linker histone in the context of other nuclear proteins. Although intriguing roles for plant linker histones are beginning to emerge, much of our current understanding comes from work in animal systems. Many unanswered questions remain and additional work is required to fully elucidate the complex processes mediated by linker histones in plants.

Keywords: DNA methylation; chromatin; development; differentiation; gene regulation; high mobility group proteins.; histone H1; imprinting; linker histone; posttranslational modifications.

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Figures

Figure 1.
Figure 1.
Linker Histone Structure. The well-conserved globular domain contains three α-helices (green) and two β-sheets (blue) (Ramakrishnan et al., 1993). The C-terminal and N-terminal domains are unstructured.
Figure 2.
Figure 2.
Linker Histones Are Sequentially Phosphorylated during the Cell Cycle. Indicated phosphorylation events were determined by mass spectrometry and immunolocalization studies of human cell cultures (Daujat et al., 2005; Sarg et al., 2006; Happel et al., 2009; Talasz et al., 2009; Zheng et al., 2010; Chu et al., 2011; Hergeth et al., 2011; Kamieniarz et al., 2012). All phosphorylation events for any H1 variant are shown. For H1 variant-specific phosphorylation, see Supplemental Table 1.
Figure 3.
Figure 3.
Expression of H1 Variants and Their Possible Contribution to Cell-Cycle Control. (A) Microarray expression levels of Arabidopsis H1 variants and core histone H4 in the shoot apex and leaves of various ages (www.weigelworld.org/resources/microarray/AtGenExpress/) (Schmid et al., 2005). The expression of H1.3 is relatively low in the apex and young leaves, but it becomes more highly expressed in the differentiated nondividing tissue of older leaves. (B) A speculative model where increased abundance of H3.3, which is depleted in CDK phosphorylation sites, inhibits the cell cycle in response to drought or differentiation.
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