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Using a poly(ADP-ribose) binding assay on protein blots we examined the ability of rat testis histone H1 variants to establish non-covalent interactions with the polymer. All the H1 variants bound ADP-ribose polymers; the binding was salt resistant and highly specific, occurring even in the presence of a large excess of competitor DNA. A comparison among the H1 variants showed that H1t has the highest affinity for poly(ADP-ribose). Long and branched poly(ADP-ribose) molecules were found to be preferentially involved in the interaction with the histone variants. The results further corroborate the concept that non-covalent interactions of poly(ADP-ribose) with target proteins may constitute an important mechanism to modulate chromatin structure.
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