Nuclear protein modification and chromatin substructure. 2. Internucleosomal localization of poly(adenosine diphosphate-ribose) polymerase

Definitive evidence for poly(ADP-Rib) polymerase activity is localized within internucleosomal "linker" regions of HeLa cell chromatin is presented. This evidence was based on the following criteria: the enzyme activity did not coincide with the position of core particles in a sucrose grad...

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Bibliographic Details
Published in:Biochemistry (Easton) 1978-08, Vol.17 (17), p.3501-3504
Main Authors: Giri, Chandrakant P, West, Michael H. P, Ramirez, Michele L, Smulson, Mark
Format: Article
Language:English
Subjects:
Cell Nucleus - enzymology
Chromatin - enzymology
DNA, Neoplasm - metabolism
HeLa Cells - enzymology
Molecular Weight
NAD+ Nucleosidase - metabolism
Poly(ADP-ribose) Polymerases - metabolism
Subcellular Fractions - enzymology
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Summary:Definitive evidence for poly(ADP-Rib) polymerase activity is localized within internucleosomal "linker" regions of HeLa cell chromatin is presented. This evidence was based on the following criteria: the enzyme activity did not coincide with the position of core particles in a sucrose gradient but was displaced to that part of the gradient which is enriched in monomers with linker regions. This was not due to dimer contamination, since resedimentation did not affect the enzyme activity in relation to the monomer. A new method of assaying enzyme activity directly in polyacrylamide gels following the separation of monomers and dimers showed that only dimers and monomers with linker regions contained activity. When dimers were digested, the enzyme activity moved from the dimer to the monomer with linker.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00610a012