In:
FEBS Letters, Wiley, Vol. 290, No. 1-2 ( 1991-09-23), p. 181-185
Abstract:
6‐Nitroso‐ 1,2‐benzopyrone, an oxidation product of 6‐amino‐ 1,2‐benzopyrone, binds to the DNA‐recognizing domain of the ADP‐ribose transferase protein and preferentially destabilizes Zn 2+ from one of the two zinc finger polypeptide complexes present in the intact enzyme, as determined by the loss of 50% of 65 Zn 2+ from the 65 Zn 2+ ‐isolated protein molecule, coincidental with the loss of 99% of enzymatic activity. The 50% zinc‐deficient enzyme still binds to a DNA template. consisting of a 17‐mer DNA primer annealed to M 13 positive strand, resulting in the blocking of DNA synthesis by the Klenow fragment of Pol I, Auto‐poly‐ADP‐ribosylated ADP‐ribose transferase, which is the probable physiological state of this protein in intact cells, does not bind to primer‐template DNA and does not block DNA synthesis by the Klenow fragment. On the basis of this in vitro model it is proposed that molecules which inhibit or inactivate ADP‐ribose transferase in intact cells can induce significant alteration in DNA structure and replication.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(91)81255-7
Language:
English
Publisher:
Wiley
Publication Date:
1991
detail.hit.zdb_id:
1460391-3
SSG:
12
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