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Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure.
Open accessAbstract
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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Metadata
- Authors
- Poirier, G. G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C., & Mandel, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1982-06
- Volume
- 79
- Issue
- 11
- Pages
- 3423-3427
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2037316481
- Cited by
- 515
- References
- 0
- FWCI
- 8.02
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Poirier, G. G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C., & Mandel, P. (1982). Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.79.11.3423
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