Poly(ADP-ribose) binding properties of histone H1 variants.
Using a poly(ADP-ribose) binding assay on protein blots we examined the ability of rat testis histone H1 variants to establish non-covalent interactions with the polymer. All the H1 variants bound ADP-ribose polymers; the binding was salt resistant and highly specific, occurring even in the presence of a large excess of competitor DNA. A comparison among the H1 variants showed that H1t has the highest affinity for poly(ADP-ribose). Long and branched poly(ADP-ribose) molecules were found to be preferentially involved in the interaction with the histone variants. The results further corroborate the concept that non-covalent interactions of poly(ADP-ribose) with target proteins may constitute an important mechanism to modulate chromatin structure.
Department of Organic and Biological Chemistry, University Federico II, Naples, Italy.
M
M
Malanga
L
L
Atorino
F
F
Tramontano
B
B
Farina
P
P
Quesada
D004247:DNA / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K; D006657:Histones / Q000737:chemistry* / Q000145:classification; D011064:Poly Adenosine Diphosphate Ribose / Q000138:chemical synthesis / Q000737:chemistry*
D006657:Histones; D011064:Poly Adenosine Diphosphate Ribose; D004247:DNA; D019286:Endopeptidase K