Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.56 (caspase-3)
35,750 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In an earlier study, intracellular accumulation of metabolites such as pyruvate and citrate in Xanthomonas campestris pv. glycines (Xcg) was found to result in a caspase dependent stationary phase rapid cell death (RCD). In the present study, the presence of poly ADP-ribose polymerase (PARP)-like activity associated with caspase-3-like protein of Xcg is reported. This activity was found to be responsible for depletion of cellular NAD(+) levels in RCD-promoting media such as Luria-Bertani medium and starch medium fortified with citrate. Addition of PARP-specific inhibitors such as 3-aminobenzamide to RCD-promoting media restored the intracellular NAD(+) levels and thereby prevented RCD. The inherent association of PARP-like activity with the caspase protein was demonstrated by PARP cellular assay, immuno-precipitation and Western analysis. A truncated polysaccharide deacetylase gene having a caspase-like domain was cloned. The expressed protein though found to be inactive, cross-reacted with human caspase and PARP antibodies. This is the first report demonstrating the presence of a PARP-like activity in a prokaryote and its involvement in cell death.
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PMID:Xanthomonas caspase displays an inherent PARP-like activity. 1752 58