Abstract:
:When rat pancreatic polynucleosomes were poly(ADP-ribosyl)ated with purified calf thymus poly(ADP-ribose) polymerase and examined by electron microscopy, a relaxation of their native zigzag structure was observed. At high ionic strengths control nucleosomes condensed into 250-A-thick fibers, but poly(ADP-ribosyl)ated polynucleosomes did not; they showed a close resemblance to chromatin depleted of histone H1. The relaxed state of poly(ADP-ribosyl)ated polynucleosomes was also confirmed by sedimentation velocity analysis. Histone H1 was found to be the major histone acceptor of poly(ADP-ribose). Poly(ADP-ribose) linked to histone H1 did not seem to cause its dissociation from the chromatin, but it impaired significantly its effect on chromatin condensation.
journal_name
Proc Natl Acad Sci U S Aauthors
Poirier GG,de Murcia G,Jongstra-Bilen J,Niedergang C,Mandel Pdoi
10.1073/pnas.79.11.3423subject
Has Abstractpub_date
1982-06-01 00:00:00pages
3423-7issue
11eissn
0027-8424issn
1091-6490journal_volume
79pub_type
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