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Review
. 2017 Apr;95(2):171-178.
doi: 10.1139/bcb-2016-0097. Epub 2016 Jun 29.

Linker histones: novel insights into structure-specific recognition of the nucleosome

Amber R Cutter  1   1 , Jeffrey J Hayes  1   1
Affiliations
Review

Linker histones: novel insights into structure-specific recognition of the nucleosome

Amber R Cutter et al. Biochem Cell Biol. 2017 Apr.

Abstract

Linker histones (H1s) are a primary component of metazoan chromatin, fulfilling numerous functions, both in vitro and in vivo, including stabilizing the wrapping of DNA around the nucleosome, promoting folding and assembly of higher order chromatin structures, influencing nucleosome spacing on DNA, and regulating specific gene expression. However, many molecular details of how H1 binds to nucleosomes and recognizes unique structural features on the nucleosome surface remain undefined. Numerous, confounding studies are complicated not only by experimental limitations, but the use of different linker histone isoforms and nucleosome constructions. This review summarizes the decades of research that has resulted in several models of H1 association with nucleosomes, with a focus on recent advances that suggest multiple modes of H1 interaction in chromatin, while highlighting the remaining questions.

Keywords: ADN; DNA; histone de liaison; linker histone; nucleosome; nucléosome.

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Figures

Figure 1
Figure 1. Linker histone family and structure
a. Phlyogram generated from multiple sequence alignment of indicated H1 sequences, both generated in CLC Sequence Viewer 7.0.2 from sequences obtained with the following Uniprot accession numbers: P02259, 78707158, P22844, P07305, P07305-2, 3878755, 4885373, 1426823, 4885375, 9845257, 4885377, 254588110, 4885379, 13430890, 4885381, 21426893, 5174449, 24475863, 19923865, 112807207, 20544168. The inferred evolutionary relationships show closer relationship of subtype across species than to other subtypes in the same species. b. Linker histone tripartite structure: structured (PDB ID: 1HST) globular domain (G-green), is flanked by a short N-terminal domain (NTD-black), and long C-terminal domain (CTD-grey), both unstructured.
Figure 2
Figure 2. Potential mechanism for H1 binding mode influence on chromatin compaction
Model shows the 3-contact and 2-contact binding interactions might lead to more or less condensed chromatin.
See this image and copyright information in PMC

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