Disease relevance of PARP

• The expression of these two forms of PARP in E. coli demonstrated that while PARP II has the catalytic NAD-binding domain and DNA-binding domain it is enzymatically inactive [1].

High impact information on PARP

• The Ced-3-related protease CPP-32 is cleaved during the late stages of apoptosis in this system and after PARP cleavage [2].
• We show that maturation-promoting factor (Cyclin B/cdc2) cannot itself be responsible for the phosphorylation and activation of PARP in maturing X. laevis eggs [3].
• We have examined the enzyme activity of PARP in oocytes and eggs of Xenopus laevis [3].
• Comparison of the PARP aa sequences among these species showed conservation of two zinc-finger motifs in the DNA-binding domain, and an NAD-binding motif and a Rossmann fold in the catalytic domain [4].
• X. laevis PARP shares 74, 83, 73, 78 and 42% aa sequence homology with the human, bovine, mouse, chicken and Drosophila melanogaster PARPs, respectively [4].

Biological context of PARP

• These experiments provide direct biochemical evidence that Bcl-2 protects against apoptosis, at least in part, by regulating the activation of a series of apoptotic proteases that cleave PARP and other substrates [2].
• Together, these results demonstrate that the enzyme activity of PARP in X. laevis oocytes and eggs is regulated by post-translational, covalent phosphorylation [3].
• The PARP gene consisted of six translatable exons and spanned more than 50 kb [1].
• A deletion mutant of PARP gene could grow to the end of embryogenesis but did not grow to the adult fly [1].

Analytical, diagnostic and therapeutic context of PARP

• Incubation of maturing X. laevis eggs with radioactive inorganic phosphate and subsequent immunoprecipitation demonstrate that the PARP protein is phosphorylated in vivo [3].

References