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Destabilization of Zn2+ coordination in ADP-ribose transferase (polymerizing) by 6-nitroso-1,2-benzopyrone coincidental with inactivation of the polymerase but not the DNA binding function
- Source :
- FEBS Letters. (1-2):181-185
- Publisher :
- Published by Elsevier B.V.
-
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 Zn2+ from one of the two zinc finger polypeptide complexes present in the intact enzyme, as determined by the loss of 50% of 65Zn2+ from the 65Zn2+-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.
- Subjects :
- DNA polymerase
DNA polymerase II
Molecular Sequence Data
Oligonucleotides
Biophysics
Poly(ADP-ribose) Polymerase Inhibitors
Biochemistry
DNA polymerase delta
Coumarins
Structural Biology
Zinc finger
6-Nitroso-1.2-benzopyrone
Genetics
Molecular Biology
Replication protein A
DNA clamp
Base Sequence
biology
Chemistry
DNA replication
DNA
Cell Biology
Molecular biology
DNA-Binding Proteins
Zinc
biology.protein
DNA polymerase I
DNA polymerase mu
ADP-ribose transferase
Nitroso Compounds
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1-2
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....dbf971c6ac77f6b6809e320ab5a96228
- Full Text :
- https://doi.org/10.1016/0014-5793(91)81255-7