The Key Involvement of Poly(ADP-Ribosylation) in Defense Against Toxic Agents: Molecular Biology Studies
Abstract
Our laboratory, during an earlier AFOSR granting period, was the first to isolate and clone a full-length cDNA for this enzyme. We also showed that this cDNA, in an appropriate vector, can be expressed in eukaryotic cells above endogenous levels. Accordingly, our laboratory is capable of performing direct experiments, utilizing recombinant DNA techniques, to test for the role of this enzyme in DNA repair and recovery from toxic agents during the renewal period. For example, we propose to construct expression vectors containing alterations in the active site and the DNA binding domain of PADPRP and to eventually stably integrate these into eukaryotic cells such that expression of these 'analog' PADPRPs will be expressed. Through the use of several of these mutants that we have already expressed in E. coli during the past granting period, the modulation of PADPRP structure should allow us to learn considerably more about the mechanism and role of this enzyme in cells exposed to stressful environments
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 29, 1993
- Accession Number
- ADA265715
Entities
People
- Mark E. Smulson
Organizations
- Georgetown University