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. 2010 Jul 2;285(27):20891-6.
doi: 10.1074/jbc.M110.108639. Epub 2010 May 5.

Nucleosome interaction surface of linker histone H1c is distinct from that of H1(0)

Eric M George  1 , Tina Izard, Stephen D Anderson, David T Brown
Affiliations

Nucleosome interaction surface of linker histone H1c is distinct from that of H1(0)

Eric M George et al. J Biol Chem. .

Abstract

The fully organized structure of the eukaryotic nucleosome remains unsolved, in part due to limited information regarding the binding site of the H1 or linker histone. The central globular domain of H1 is believed to interact with the nucleosome core at or near the dyad and to bind at least two strands of DNA. We utilized site-directed mutagenesis and in vivo photobleaching to identify residues that contribute to the binding of the globular domain of the somatic H1 subtype H1c to the nucleosome. As was previously observed for the H1(0) subtype, the binding residues for H1c are clustered on the surface of one face of the domain. Despite considerable structural conservation between the globular domains of these two subtypes, the locations of the binding sites identified for H1c are distinct from those of H1(0). We suggest that the globular domains of these two linker histone subtypes will bind to the nucleosome with distinct orientations that may contribute to higher order chromatin structure heterogeneity or to differences in dynamic interactions with other DNA or chromatin-binding proteins.

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Figures

FIGURE 1.
FIGURE 1.
H1c has a significantly lower affinity for chromatin than H10 does. FRAP analysis of wild type H1c-GFP and H10-GFP is shown. Values are the means ± S.D. (error bars) from nine independent measurements for each. Values for the half-time of recovery (t50) values were determined as described previously (30).
FIGURE 2.
FIGURE 2.
FRAP analysis of mutant and wild type (WT) H1c-GFP. a, sequence alignment of the globular domains of H1c and H10. Residues determined to contribute to binding are indicated by a + sign above or below the sequence. Data for H1c are from this study. Data for H10 are from ref. . Solid lines between the sequences indicate the position of α-helices. b–f, FRAP analysis of mutants containing single point mutations in putative binding residues. For clarity, error bars are not displayed but were similar to those shown in Fig. 1. g, summary of t50 values. Asterisks indicate p < 10−4.
FIGURE 3.
FIGURE 3.
Map of the interaction surface of the globular domain of H1c and comparison with that of H10. a, interaction surface of the globular domain of H1c based on the NMR structure of the chicken ortholog (31) (Protein Data Bank code 1GHC) and the data from Fig. 2 and Table 1. Red, binding residues; blue, nonbinding residues. b, interaction surface of the globular domain of H10 based on the crystal structure of the chicken H5 (11) (Protein Data Bank code 1HST_A) taken from data in Ref. . Red, binding residues; blue, nonbinding residues.
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