PMID:21112350

Citation	Orth, JH, Schorch, B, Boundy, S, Ffrench-Constant, R, Kubick, S and Aktories, K (2011) Cell-free synthesis and characterization of a novel cytotoxic pierisin-like protein from the cabbage butterfly Pieris rapae. Toxicon 57:199-207
Abstract	Pierisin-like proteins comprise a growing family of ADP-ribosyltransferases expressed in various species of white butterflies. The prototype pierisin-1 from the cabbage butterfly, Pieris rapae, was identified as a potent apoptosis-inducing agent, acting on various types of carcinoma cell lines by mono-ADP-ribosylation of DNA. The characterization of pierisin-like proteins is hampered by its potent toxicity, which prevents its expression as a recombinant protein in Escherichia coli. Here we characterized a new member of the pierisin protein family named pierisin-1b, which was cloned from P. rapae. Pierisin-1b consists of 849 amino acids residues and shares 63%-91% identity with already described pierisins. For expression of pierisin-1b a novel in vitro translation system was utilized. Obtained protein exhibits specific ADP-ribosyltransferase activity on deoxyguanosine residues of DNA leading to induction of apoptosis and cell death.
Links	PubMed Online version:10.1016/j.toxicon.2010.11.011
Keywords	ADP Ribose Transferases/chemistry; ADP Ribose Transferases/genetics; ADP Ribose Transferases/pharmacology; Amino Acid Sequence; Animals; Apoptosis/drug effects; Butterflies/chemistry; Cell-Free System; Cloning, Molecular; Cytotoxins/chemistry; Cytotoxins/genetics; Cytotoxins/pharmacology; HeLa Cells; Humans; Insect Proteins/chemistry; Insect Proteins/genetics; Insect Proteins/pharmacology; Molecular Sequence Data; Sequence Alignment
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
PIERA:PRSN		GO:0030592: DNA ADP-ribosylation	ECO:0000314:		P		DNA-ADP-ribosylation activity of pierisin-1b is demonstrated in Figure 3A which shows that pierisin-1b catalyzed the 32P-labeling of DNA.	complete CACAO 12933

References

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