Figure 5.

Protein sequence alignment of O. dioica histone variants, including identified PTMs. Dots indicate identical residues to the top reference sequence for each group. Histone secondary structure motifs are indicated above the reference sequences: loops (Lx), N- and C-terminal tails of the core histones (lines), alpha helices (rectangles), N-terminal tail of H1 (dashed line), H1 globular domain (black line), H1 C-terminal region (dotted line). For H2B and H2A, a vertebrate consensus sequence was generated by aligning canonical histones from chicken, zebrafish, Xenopus and human: "x" indicates variable residues in the consensus. PTMs identified by mass-spectrometry are shaded in different colors as indicated in the key: Me1-3, mono- to tri-methylation, Ac, acetylation; Ub, ubiquitinylation; put. phospho. sites, putative phosphorylation sites. PTMs previously reported from vertebrates are indicated in the consensus sequences. Novel O. dioica modifications are shaded without a corresponding PTM-tag in the reference sequence. Some intra- and inter-nucleosomal interaction sites are indicated in different colored bold with underlines: A) H3 α2 interaction (black) with α2 of H4. B) H4 residues 16-25 (black) interact with the acidic patch of H2A. C) H2B residues (black) interacting with the α2 of H2A and H2B residues (green) that interact as part of a 4-helix bundle with H4. D) H2A residues within L1 that form the H2A self-dimerization domain (blue), residues interacting with the α2 of H2B (black), docking domain that makes contact with the H3-H4 tetramer (bracket) and residues in the acidic patch on the nucleosome disc surface (orange).

Moosmann et al. BMC Evolutionary Biology 2011 11:208   doi:10.1186/1471-2148-11-208
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