Abstract
Poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase activities were both investigated in chicken erythroblasts transformed by Avian Erythroblastosis Virus. Respectively 21% and 58% of these activities were found to be present in the post-mitochondrial supernatant (PMS). Fractionation of the PMS on sucrose gradients and poly(A+) mRNA detection by hybridization to [3H] poly(U) show that cytoplasmic poly(ADP-ribose) polymerase is exclusively localized in free mRNP. The glycohydrolase activity sedimented mostly in the 6 S region but 1/3 of the activity was in the free mRNP zone. Seven poly(ADP-ribose) protein acceptors were identified in the PMS in the Mr 21000–120000 range. The Mr 120000 protein corresponds to automodified poly(ADP-ribose) polymerase. A Mr 21000 protein acceptor is abundant in PMS and a Mr 34000 is exclusively associated with ribosomes and ribosomal subunits. The existence of both poly(ADP-ribose) polymerase and glycohydrolase activities in free mRNP argues in favour of a role of poly(ADP-ribosylation) in mRNP metabolism. A possible involvement of this post translational modification in the mechanisms of repression-derepression of mRNA is discussed.
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Abbreviations
- ADP-ribose:
-
adenosine (5′) diphospho(5)-β-D ribose
- poly(ADP-ribose):
-
polymer of ADP-ribose
- mRNP:
-
messenger ribonucleoprotein particles
- PMSF:
-
phenylmethylsulfonyl fluoride
- LDS:
-
lithium dodecyl sulfate
- TCA:
-
trichloroacetic acid
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Thomassin, H., de Sa, C.M., Scherrer, K. et al. Cytoplasmic poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase in AEV-transformed chicken erythroblasts. Mol Biol Rep 13, 35–44 (1988). https://doi.org/10.1007/BF00805637
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DOI: https://doi.org/10.1007/BF00805637