Asymmetric lateral distribution of unshielded phosphate groups in nucleosomal DNA and its role in DNA bending.
- 1 March 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (3) , 1118-1121
- https://doi.org/10.1073/pnas.76.3.1118
Abstract
We suggest that an asymmetric charge neutralization of DNA phosphate groups produces part of the driving force for nucleosome folding. In nucleosome core particle DNA, many of the phosphate groups are neutralized by histones, and a lateral alignment of these histones along the core DNA has been demonstrated [Mirzabekov A. D., Shick, V. V., Belyavsky, A. V. & Bavykin, S. G. (1978) Proc. Natl. Acad. Sci. USA 75, 4184--4189]. Histones appear to shield DNA phosphatases asymmetrically at one side of the surface of the DNA double helix along all its length inside the core. The external side of the DNA helix remains unneutralized. The electrostatic repulsion between negatively charged unneutralized phosphates may fold the nucleosomal DNA towards the side occupied by histones.This publication has 35 references indexed in Scilit:
- DNA condensation with polyaminesJournal of Molecular Biology, 1978
- Changes of nucleosome frequency in nucleolar and non-nucleolar chromatin as a function of transcription: an electron microscopic studyCell, 1978
- The compaction of DNA helices into either continuous supercoils or folded-fiber rods and toroidsCell, 1978
- DNA folding in the nucleosomeJournal of Molecular Biology, 1977
- Mapping DNAase I-susceptible sites in nucleosomes labeled at the 5′ endsCell, 1976
- Comparative organization of active transcription units in Oncopeltus fasciatusCell, 1976
- Kinky helixNature, 1975
- Folding of the DNA double helix in chromatin-like structures from simian virus 40.Proceedings of the National Academy of Sciences, 1975
- Reactive properties of the amino groups of histones in calf thymus chromatinJournal of Molecular Biology, 1974
- Model nucleohistones: The interaction of F1 and F2al histones with native T7 DNAJournal of Molecular Biology, 1971