ADP-Ribosylation of Topoisomerase II in Physiological Conditions
ADP-ribosylation is known to play an important role in the modulation of chromatin structure, possibly by changing the affinity of histones to DNA and by interfering with the activity of enzymes which are responsible for condensation and decondensation processes (1, 2). Several nuclear proteins have been found to be ADP-ribosylated in reconstituted systems (for a review, see 1). However, it is not yet clear which are the real acceptors in physiological conditions. In fact, beside poly(ADP-ribose)polymerase itself (3, 4), only histones (5), topoisomerase I (6, 7) and high and low mobility group proteins (8) have been recognized to be modified by poly(ADP-ribose) in intact eukaryotic systems.
KeywordsAgarose Boronate Glycine Ribose Phenylboronate
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