QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

Help viewing high resolution images Return to article

Fig. 2. Schematic representation of human histone poly(ADP-ribosyl)ation sites. The positions of covalent modification sites (branched structures) for human histones H1 and H2B have been predicted from corresponding rat coordinates (Riquelme et al., 1979; Ogata et al., 1980a; Ogata et al., 1980b). The amino acid sequences of non-covalent poly(ADP-ribose)-association sites identified from in vitro studies are shown for H2A, H2B, H3 and H4 (Pleschke et al., 2000). Putative binding sites are shown for H1, macroH2A and CENP-A. They correspond to the sequence best matching the consensus–KRXHXBXHHBBHHBX– (Pleschke et al., 2000), where H is a hydrophobic amino acid, B is a basic amino acid and X is any amino acid. There may be more than one poly(ADP-ribose)-binding site in H1. Positions of the histone fold (ovals) and tail regions are according to Arents and Moudrianakis (Arents and Moudrianakis, 1995) for H2A, H2B, H3 and H4 and approximated for H1, macroH2A and CENP-A. The macro domain of macroH2A is represented by a diamond. (Human histone sequence accession numbers: H1.2: P16403; H2A: P02261; macroH2A2: Q9P0M6; H2B: P02278; H3: P16106; CENP-A: P49450; H4: P02304.)

Return to article