Proceedings of the National Academy of Sciences · 1982 · 511 citations · 29 references
Life SciencesBiochemistryMolecular BiologyChromatin BiologyChromatin StructureStructural BiologyChromatinChromatin BiophysicsChromosome CondensationHistone ProteinsNucleosome OrganizationNucleosome StructureChromatin Fiber OrganizationChromatin Fiber StructureFibersHistone H1 AssociationHistone H1 BindingSedimentation AnalysisSedimentation Velocity
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.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Haider Raza, Annie John, Abderrahim Nemmar · Cellular Physiology and Biochemistry · 2013 · 47.3K citations · Full text
(ADP-ribose)n participates in DNA excision repair
Barbara W. Durkacz, Olusesan Omidiji, Douglas A. Gray et al. · Nature · 1980 · 1.1K citations