Binding of topo I to PARP I - antibody immunocomplex.
It is frequently quoted in the literature that the cellular role of PARP I is its participation in the recognition of single strand breaks of genomic DNA (l.c.1). Although there is little doubt that PARP I can be made to respond powerfully as an factor in the recognition of DNA damage, it seems unlikely that this auxilliary, or telelogically defined, role of this highly abundant nuclear protein exhausts its physiologic cellular function. We have reported that Topo I is greatly activated by its association with PARP I (J Mol Med 5: 533-540, 2000). Translation of this in vitro model experiments to physiologic conditions was accomplished by the demonstration of the quantitative binding of Topo I to a PARP I - antibody complex, as reported here. This experiment demonstrates for the first time that the colligative action of PARP I can regulate a highly significant cellular process, the control of readability of genomic DNA, i.e., gene expression, without the artificiality of induced DNA damage.
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Document Type: Research Article
Affiliations: Department of Medical Biochemistry, Semmelweiss University, Budapest, Hungary.
Publication date: August 1, 2000
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- The International Journal of Molecular Medicine is a monthly, peer-reviewed journal devoted to the publication of high quality studies related to the molecular mechanisms of human disease. The journal welcomes research on all aspects of molecular and clinical research, ranging from biochemistry to immunology, pathology, genetics, human genomics, microbiology, molecular pathogenesis, molecular cardiology, molecular surgery and molecular psychology.
The International Journal of Molecular Medicine aims to provide an insight for researchers within the community in regard to developing molecular tools and identifying molecular targets for the diagnosis and treatment of a diverse number of human diseases.
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