The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms
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* Corresponding author: Jan Postberg jan.postberg@uni-wh.de
1 Institute of Cell Biology, University of Witten/Herdecke, Witten, Germany
2 Department of Biology, Hamilton College, Hamilton, NY, USA
BMC Evolutionary Biology 2010, 10:259 doi:10.1186/1471-2148-10-259
Published: 25 August 2010Additional files
Additional file 1:
Consensus sequence cartoon of histone H3 (long branching sequences removed) and aligned protein sequences of 128 H3 variants. Amino acid positions refer to human H3.1. Identical sites are shaded in black, similar residues are shaded in light grey. The positions of four helix motifs within the histone fold domain and the putative chaperone recognition domain are marked at the top of the alignment.
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Additional file 2:
Phylogenetic tree of eukaryotic life (simplified after [23]). The position of selected species is highlighted.
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Additional file 3:
FASTA formatted histone H3 variant sequence alignment.
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Additional file 4:
Overview about the most frequent residue alterations in various ancestral state sequences of histone H3 (compare Figure 3). Variable sites are highlighted (*); symbols beneath list the most frequent amino acid variations. Outgroup taxons used for ancestral state reconstruction a displayed within brackets for each clade.
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Additional file 5:
The alignment contains some exemplary N-terminal chromodomain sequences of putative Hp1-like proteins from putatively early branching eukaryotes, which possess a set of conserved residues (*) formally required for ARKme3S/T binding. Residues identical in 85% of all sequences are shaded black; residues similar in 85% of all sequences are shaded grey. Notably, in three Trichomonas vaginalis sequences a C-terminal chromoshadowdomain could be recognized (C+CS).
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