A nuclear protein-modifying enzyme is responsive to ordered chromatin structure
- 1 January 1978
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 5 (8) , 2775-2788
- https://doi.org/10.1093/nar/5.8.2775
Abstract
Poly (ADP-ribose) polymerase, a nuclear protein-modifying enzyme, binds to the internucleosomal linker region of chromatin, although it modifies certain core nucleosomal histones in addition to histone H1. The activity per unit of DNA chromatin changes with the nucleosome repeat number. It reaches a maximum on chromatin of 8-10 nucleosomes in length. As the complexity of chromatin with respect to nucleosome repeat number and compactness increases, a decline and stabilization of specific activity is noted. The difference in specific activity is maintained through resedimentation and dialysis of particles. It does not appear due to differences in polymer chain length or differential degradation of poly (ADP-ribose). The data suggest a relationship between ADP-ribosylation and chromatin organization and vice versa.Keywords
This publication has 13 references indexed in Scilit:
- Properties of the Complex between Histone H1 and Poly(ADP‐ribose) Synthesised in HeLa Cell NucleiEuropean Journal of Biochemistry, 1977
- Higher order coiling of DNA in chromatinCell, 1977
- Two-dimensional electrophoretic analysis of polynucleosomes.Journal of Biological Chemistry, 1977
- Adenosine Diphosphoribosylation of Certain Basic Chromosomal Proteins in Isolated Trout Testis NucleiEuropean Journal of Biochemistry, 1977
- Involvement of histone H1 in the organization of the chromosome fiber.Proceedings of the National Academy of Sciences, 1977
- Poly(adenosine diphosphate-ribose) polymerase: the distribution of a chromosome-associated enzyme within the chromatin substructureBiochemistry, 1977
- ‘Single-stranded’ DNA from φX174 and M13 is cleaved by certain restriction endonucleasesNature, 1975
- Natural occurrence of poly(ADP-ribosyl) histones in rat liver.Proceedings of the National Academy of Sciences, 1975
- Detection of two restriction endonuclease activities in Haemophilus parainfluenzae using analytical agarose-ethidium bromide electrophoresisBiochemistry, 1973
- Studies on poly(adenosine diphosphate-ribose)Archives of Biochemistry and Biophysics, 1971