Accession Number : ADA265715


Title :   The Key Involvement of Poly(ADP-Ribosylation) in Defense Against Toxic Agents: Molecular Biology Studies


Descriptive Note : Annual technical rept. 1 Apr 92-31 Mar 93,


Corporate Author : GEORGETOWN UNIV WASHINGTON DC SCHOOL OF MEDICINE


Personal Author(s) : Smulson, Mark E


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a265715.pdf


Report Date : 29 Apr 1993


Pagination or Media Count : 8


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


Descriptors :   *BIOCHEMISTRY , *ENZYMES , *DEOXYRIBONUCLEIC ACIDS , LABORATORY TESTS , TOXIC AGENTS , GENES , MUTAGENS , IONIZING RADIATION , PESTICIDES , DISEASE VECTORS , RECEPTOR SITES(PHYSIOLOGY) , MEDICAL RESEARCH , MICE , MOLECULAR BIOLOGY , ESCHERICHIA COLI , AIR FORCE RESEARCH , HUMANS


Subject Categories : Biochemistry
      Genetic Engineering and Molecular Biology
      Medicine and Medical Research


Distribution Statement : APPROVED FOR PUBLIC RELEASE