Poly(ADP-ribose) binding properties of histone H1 variants

Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins

“…As expected, PAR bound strongly to the native effector domain (M; Fig. 1A), and a 7-fold excess of competing poly(A) (11) or a 10-fold excess of sonicated calf thymus DNA (17) did not reduce PAR binding (cf. "Experimental Procedures").…”

“…In the presence of a 10-fold excess (w/w) of competing calf thymus DNA, PAR binding to immobilized polypeptides with a PAR-binding motif is not reduced, whereas a 100-fold excess DNA reduces this binding by ϳ50% (17). Similar results were obtained when a 27-nucleotide double-stranded DNA fragment was used for competition experiments.…”

“…Although proteins and polypeptides immobilized on nitrocellulose still bind sonicated calf thymus DNA, this binding is not resistant to washing with 1 M NaCl (17). In the presence of a 10-fold excess (w/w) of competing calf thymus DNA, PAR binding to immobilized polypeptides with a PAR-binding motif is not reduced, whereas a 100-fold excess DNA reduces this binding by ϳ50% (17).…”

Poly(ADP-ribosyl)ation and Epigenetics: Is CTCF PARt of the Plot?

“…Moreover, histone H1 interacts with PAR much more strongly than with the DNA itself suggesting the interesting possibility that the PARlation of H2B could indirectly modulate the affinity between the DNA and any neighbouring histone H1. 30,31 On a similar note, free PAR molecules are also able to affect directly the formation of H1-H1 oligomers and therefore regulate processes of chromatin remodeling. 32 Taken together, these data suggest a link between PARlation and epigenetic processes.…”

Mammalian Spermatogenesis, DNA Repair, Poly(ADP-ribose) Turnover: the State of the Art

“…At that time the presence of more than the 116kDa PARP was unconceivable, being the second enzyme, PARP2, discovered at the end of '90s (Ame Babiychuck et al, 1998). In rat testis most PARP activity was found in isolated seminiferous tubules (Quesada et al, 1989) and among linker histone variants, the rat testis specific H1t was preferentially modified with poly(ADP-ribose) (Faraone Mennella et al, 1999;Malanga et al, 1998). In a study with differently-aged rats, it was found that in isolated intact nuclei of testis from 8-day-old animals (only spermatogonia present in seminiferous tubules), poly(ADPribosylation) of nuclear proteins was very low, increased significantly by 16-day (pachytene spermatocytes appear) and reached adult proportions by 32 days (condensing spermatids present), Figure 1B (Quesada et al, 1989).…”