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. 2013 Jan 5;6:1. doi: 10.1186/1756-8935-6-1

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Copyright ©2013 Kassner et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Full-length H1.4 is methylated at six lysine residues by SET7/9. (A) Mutation of the four lysine residues K159, K171, K177 and K192 (K4R) in wild-type (WT) H1.4 reduces SET7/9-dependent methylation. The additional mutation of K121 and K129 (K6R) abolishes methylation of full-length H1.4 by SET7/9. (B) H1.4 is efficiently PARylated after methylation by SET7/9. H1.4 was first incubated with S-adenosyl-L-(methyl-¹⁴C) methionine (¹⁴C-SAM) and glutathione-S-transferase (GST) or SET7/9 and then incubated with ADP-ribosyltransferase-D1 (ARTD1) in the presence or absence of cold nicotinamide adenine dinucleotide (NAD)⁺. (C) H1.4 K6R is still modified by ARTD1. H1.4 WT and K6R were incubated with ARTD1 in the presence of 250 μM NAD⁺. PARylation was analyzed by Western blotting.