Structural insights into the histone H1-nucleosome complex

Zhou, Bo; Feng, Hanqiao; Kato, Hidenori; Dai, Liang; Yang, Yuedong; Zhou, Yaoqi; Bai, Yawen

doi:10.1073/pnas.1314905110

Cited by 193 publications

(245 citation statements)

References 57 publications

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“…distinct for different H1 isoforms, current data support a general mode of binding in which the H1 globular domain binds near the dyad axis, with the CTD mainly contacting one linker DNA such that linker DNA is organized into a stem-like structure (Fig. 4) (32,38). In this configuration, one H1 has been proposed to link three nucleosomes and to prevent the association of additional H1 protomers, likely due to electrostatic repulsion.…”

Section: Figsupporting

confidence: 53%

“…3) (30). The globular domain adopts a winged-helix DNA binding motif (31); its interaction with DNA at the nucleosomal entry/exit points gives rise to protection of the additional ϳ20 bp (23,32). The structure of the chicken linker histone H5 in complex with a nucleosome reveals the binding of the globular domain on the nucleosome dyad axis, interacting with both The globular domain of histone H1 (purple) binds the nucleosome at the dyad.…”

Section: Linker Histonesmentioning

confidence: 99%

“…DNA linkers, whereas the Drosophila melanogaster linker histone H1 binds off-dyad (32,33). Experiments involving site-directed mutagenesis followed by determination of binding to nucleosomes in living cells have likewise led to the conclusion that the globular domains of different mouse H1 isoforms use different interaction surfaces for contacts to chromatin (34,35).…”

Section: Linker Histonesmentioning

confidence: 99%

“…(A) H1 binds near the dyad such that the CTD mainly contacts one linker segment; this creates a stem-like structure that stabilizes the nucleosome core (32,38). (B) For HMGB, interactions between the acidic CTD and the H3 N-terminal tail that exits near the dyad promote binding of HMGB to DNA; the DNA bending and underwinding induced may propagate to the nucleosome core to promote unwrapping or access to other factors (118,119).…”

Section: Figmentioning

confidence: 99%

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Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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SUMMARY Eukaryotic genomes are packaged in chromatin. The higher-order organization of nucleosome core particles is controlled by the association of the intervening linker DNA with either the linker histone H1 or high mobility group box (HMGB) proteins. While H1 is thought to stabilize the nucleosome by preventing DNA unwrapping, the DNA bending imposed by HMGB may propagate to the nucleosome to destabilize chromatin. For metazoan H1, chromatin compaction requires its lysine-rich C-terminal domain, a domain that is buried between globular domains in the previously characterized yeast Saccharomyces cerevisiae linker histone Hho1p. Here, we discuss the functions of S. cerevisiae HMO1, an HMGB family protein unique in containing a terminal lysine-rich domain and in stabilizing genomic DNA. On ribosomal DNA (rDNA) and genes encoding ribosomal proteins, HMO1 appears to exert its role primarily by stabilizing nucleosome-free regions or “fragile” nucleosomes. During replication, HMO1 likewise appears to ensure low nucleosome density at DNA junctions associated with the DNA damage response or the need for topoisomerases to resolve catenanes. Notably, HMO1 shares with the mammalian linker histone H1 the ability to stabilize chromatin, as evidenced by the absence of HMO1 creating a more dynamic chromatin environment that is more sensitive to nuclease digestion and in which chromatin-remodeling events associated with DNA double-strand break repair occur faster; such chromatin stabilization requires the lysine-rich extension of HMO1. Thus, HMO1 appears to have evolved a unique linker histone-like function involving the ability to stabilize both conventional nucleosome arrays as well as DNA regions characterized by low nucleosome density or the presence of noncanonical nucleosomes.

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Section: Figsupporting

confidence: 53%

Section: Linker Histonesmentioning

confidence: 99%

Section: Linker Histonesmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

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Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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“…Considering the key roles of H1 histone in general chromatin compaction, neither of these are strong possibilities (42). Nonetheless, we measured total cellular H1.2 following Colcemid-induced enrichment of metaphase cells.…”

Section: The Cellular H12 Levels Were Similar At Interphase and Metamentioning

confidence: 99%

The linker histone H1.2 is a novel component of the nucleolar organizer regions

Chen

Teo

Cai

et al. 2018

Journal of Biological Chemistry

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The nucleoli accumulate rRNA genes (rDNA) and are the sites of rRNA synthesis and rRNA assembly into ribosomes. During mitosis, nucleoli dissociate but nucleolar remnants remain on the rDNA loci, forming distinct nucleolar organizer regions (NORs). Little is known about the composition and structure of NORs, but upstream binding factor (UBF) has been established as its master organizer. In this study, we sought to establish new proteins in NORs. Using UBF-Sepharose to isolate UBFbinding proteins, we identified histone H1.2 as a candidate partner, but were puzzled by this observation given that UBF is known to be located predominantly in nucleoli whereas H1.2 distributed broadly among the chromatins in interphase nuclei. We then examined cells undergoing mitosis, and saw that both H1.2 and UBF were recruited into NORs in this state, reconciling the results of our UBF pulldowns. Inhibiting rRNA synthesis in interphase nuclei also induced NOR-like structures containing both UBF and H1.2. When chromosomes were isolated and spread on coverslips, NORs appeared separated from the chromosomes containing both UBF and H1.2. After chromosomes were fragmented by homogenization, intact NORs remained visible. Results collectively suggest NORs are independent structures and the linker histone H1.2 is a novel component of this structure.

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The shades of gray of the chromatin fiber

Ausió

2014

BioEssays

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The chromatin fiber consists of a string of nucleosomes connected by linker DNA regions. The hierarchy of folding of this fiber within the cell has long been controversial, and the existence of an originally described 30 nm fiber has been debated and reviewed extensively. This review contextualizes two recent papers on this topic that suggest the 30 nm fiber to be an over-simplification. The idealized model from the first study provides good insight into the constraints and histone participation in the maintenance of the fiber structure. The second paper provides a theoretical description of a more realistic view of the highly heterogeneous and dynamic chromatin organization in the in vivo setting. It is now time to abandon the highly regular "one start" solenoidal 30 nm structure and replace it with a more realistic highly dynamic, polymorphic fiber.

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Structural insights into the histone H1-nucleosome complex

Cited by 193 publications

References 57 publications

Yeast HMO1: Linker Histone Reinvented

Yeast HMO1: Linker Histone Reinvented

The linker histone H1.2 is a novel component of the nucleolar organizer regions

The shades of gray of the chromatin fiber

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