Sequential ADP-ribosylation pattern of nucleosomal histones. ADP-ribosylation of nucleosomal histones
- Resource Type
- Authors
- Claude Niedergang; Ann Huletsky; Rémy Aubin; André Fréchette; G.G. Poirier; Alain Gaudreau
- Source
- European journal of biochemistry. 146(2)
- Subject
- DNA Replication
DNA Repair
Thymus Gland
Biology
Biochemistry
Histones
NAD+ Nucleosidase
Histone H1
Histone H2A
Histone methylation
Histone H2B
Nucleosome
Animals
Histone octamer
Binding Sites
Dose-Response Relationship, Drug
NAD
Chromatin
Nucleosomes
Enzyme Activation
Histone methyltransferase
Cattle
Electrophoresis, Polyacrylamide Gel
NAD+ kinase
Poly(ADP-ribose) Polymerases
- Language
- ISSN
- 0014-2956
The pattern of nucleosomal histones poly(ADP-ribosyl)ation is changed under conditions which affect the poly(ADP-ribosyl)ation state of the enzyme. At low NAD concentrations the enzyme can poly(ADP-ribosyl)ate histones H1 and H1, H2A, A2A, and H2B. However at NAD concentrations above 10 microM the enzyme preferentially poly(ADP-ribosyl)ates histone H1 to a hyper ADP-ribosylated form. Furthermore we have observed hyper ADP-ribosylation of histone H2B at NAD concentrations of 10 microM suggesting that histone H2B can undergo the same type of ADP-ribosylation pattern as histone H1. Also at higher NAD concentrations an elongation of the polymer attached to the enzyme and other nuclear proteins takes place.