Adenosine Diphosphate Ribosylation of Chicken‐Erythrocyte Histones H1, H5 and High‐Mobility‐Group Proteins by Purified Calf‐Thymus Poly(adenosinediphosphate‐ribose) Polymerase

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Abstract
Poly(ADP-ribosylation) of histones H1, H5 and non-histone chromosomal high-mobility-group proteins HMG 1, 2, 14 and 17 from chicken erythrocytes by purified calf thymus poly(ADP-ribose) polymerase was studied using acid/urea/Triton gel electrophoresis and autoradiography. With histone H1, besides ADP-ribosylated H1 supporting short chains of polymer, the appearance of H1 dimer was observed and this reaction was dependent on NAD concentration and incubation time. In addition, highly modified and/or aggregated species of histone H1 were observed. Histone H5 was slightly ADP-ribosylated at low NAD concentrations. At higher NAD concentrations or after longer incubations the formation of H5 dimer and of more modified forms of H5 could be observed. HMG 1 and HMG 2 were ADP-ribosylated, the reaction being dependent on NAD concentration and time. Here again some discrete intermediates appeared. HMG 14 and HMG 17 were only slightly ADP-ribosylated under the experimental conditions. The purified DNA-independent poly(ADP-ribose) polymerase can catalyze the formation of H1 dimer as in nuclei and nucleosomes and H5 and HMG proteins can also be ADP-ribosylated and produce well-defined higher complexes. These modifications of nuclear proteins may provide a means of localized conformational changes of the chromatin structure in vivo.

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