Natural occurrence of poly(ADP-ribosyl) histones in rat liver.
نویسندگان
چکیده
Poly(ADP-ribose) bound to histones has been isolated from rat liver. When [14C]ribose was administered intraperitoneally to rats at a dosage of 300-750 mug (100-250 muCi)/10o g, approximately 1% of the radioactivity was recovered in the acid (5% CLCCCOOH)-INSOLUBLE MATERIAL OF THE LIVER NUCLEI 2 HR AFTER INJECTION. Of the acid-insoluble radioactivity, 4.5-9% was extractable with 0.25 N HCL. Carboxymethyl-cellulose column chromatography of the HCl-extracted material revealed that the radioactivity cochromatographed with histone subfractions f1 and, to a lesser extent, f2 and f3. Part of the protein-bound radioactivity was rendered acid-soluble by treatment with either snake venom phosphodiesterase or neutral NH2OH. From the enzyme digest, 5'-AMP and psiADP-ribose [2'-(5"-phosphoribosyl)-5'-AMP] were recovered, while the NH2OH treatment yielded ADP-ribose monomer and, presumably, oligomer. These observations indicate that ADP-ribose is attached to histones in vivo and is present both as a monomer and a polymer.
منابع مشابه
Multiple Autopoly ( ADP - ribosy 1 ) ation of Rat Liver Poly ( ADP - ribose ) Synthetase MODE
Poly(ADP4bose) synthetase of rat liver was found to catalyze automodification on multiple sites. When the synthetase was incubated with 2.4 p~ NAD for 20 s in the presence of DNA, more than 90% of ADP ribose incorporated into acid-insoluble material co-migrated with the synthetase (Mr = 108,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Incubation for longer times or at hi...
متن کاملPoly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler.
Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 in...
متن کاملPoly(ADP-ribosyl)ated chromatin domains: access granted.
The seemingly static architecture of interphase and mitotic chromatin betrays an otherwise elegantly dynamic entity capable of remodelling itself to facilitate DNA replication, transcription, repair and recombination. Remodelling of local chromatin domains in response to physiological cues proceeds, at least in part, through transient cycles of relaxation and condensation that require use of hi...
متن کامل3′-5′ Phosphoadenosine phosphate is an inhibitor of PARP-1 and a potential mediator of the lithium-dependent inhibition of PARP-1 in vivo
pAp (3'-5' phosphoadenosine phosphate) is a by-product of sulfur and lipid metabolism and has been shown to have strong inhibitory properties on RNA catabolism. In the present paper we report a new target of pAp, PARP-1 [poly(ADP-ribose) polymerase 1], a key enzyme in the detection of DNA single-strand breaks. We show that pAp can interact with PARP-1 and inhibit its poly(ADP-ribosyl)ation acti...
متن کاملEnzyme characteristics of recombinant poly(ADP-ribose) polymerases-1 of rat and human origin mirror the correlation between cellular poly(ADP-ribosyl)ation capacity and species-specific life span.
Poly(ADP-ribosyl)ation is a posttranslational modification, which is involved in many cellular functions, including DNA repair and maintenance of genomic stability, and has also been implicated in cellular and organismal ageing. We have previously reported that maximum poly(ADP-ribosyl)ation capacity in mononuclear blood cells is correlated with mammalian life span. Here we show that the differ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 72 1 شماره
صفحات -
تاریخ انتشار 1975