Structural basis of autoinhibition and activation of the DNA-targeting ADP-ribosyltransferase pierisin-1.

ABSTRACT: ADP-ribosyltransferases transfer the ADP-ribose moiety of βNAD⁺ to an acceptor molecule, usually a protein that modulates the function of the acceptor. Pierisin-1 is an ADP-ribosyltransferase from the cabbage butterfly Pieris rapae and is composed of N-terminal catalytic and C-terminal ricin B-like domains. Curiously, it ADP-ribosylates the DNA duplex, resulting in apoptosis of various cancer cells, which has raised interest in pierisin-1 as an anti-cancer agent. However, both the structure and the mechanism of DNA ADP-ribosylation are unclear. Here, we report the crystal structures of the N-terminal catalytic domain of pierisin-1, its complex with βNAD⁺, and the catalytic domain with the linker connecting it to the ricin B-like domains. We found that the catal

SUBMITTER: Oda T 

PROVIDER: S-EPMC5602402 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature