By M. E. Drets, G. A. Folle, F. J. Monteverde (auth.), Professor Dr. Günter Obe, Professor Dr. A. T. Natarajan (eds.)
Chromosomale Mutationen sind eine der m|glichen Ursachen f}r Ver{nderungen der Erbinformation. Neben grunds{tzlichen As- pekten, wie Reparaturmechanismen der Zelle oder Ursachen von Chromosomenver{nderungen, werden angewandte Aspekte, z.B. Chromosomen als Testindikatoren der Toxizit{t, behandelt.
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Example text
In addition, when histones were given the choice to associate either with DNA or preexisting polymerase-bound ADP-ribosyl polymers, they exhibited a clear preference for the polymers. This binding of histones to polymers was saturable (Realini and Althaus, unpub!. ). Taken together, these results suggest that poly(ADP-ribose)polymerase may act as a histone shuttle mechanism in chromatin, in which the catabolic counterpart, poly(ADP-ribose)glycohydrolase could assume the role of reestablishing DNA-binding of histones.
If the persisting lesions in xrs 6 are radiation-induced base damages, then one would expect an increase in the frequency of SeEs in this cell line following X-rays. When xrs 6 cells were irradiated with different doses of X-rays, a dose-dependent increase in the frequency of SeEs was obtained (Fig. 1; Darroudi and Natarajan 1987b). There was a small increase in xrs 5 cells and no increase in wild-type cells (Fig. 1). It is possible to alter the proportion of radiation-induced DNA strand breaks to base damage by altering the irradiation conditions.
Another important aspect ofthis observation is that this mechanism implies self-termination of polymer elongation, which is also attributable to the action of the polymerase itself. However, we already know that other proteins present in our in vitro system do have an impact on this termination mechanism, generating different though highly constant polymer size distributions. We speculate that the 2 Origin- CF - _ _ 3 _ 4 5 _ 678 • Fig. 5. Release of a 146-bp core DNA fragment for its association with histone H2B following incubation of the DNAhistone complex in the presence of poly(ADP-ribose )polymerase and 100 ,liM NAD.